An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis.
A subtype of non-receptor protein tyrosine phosphatases that includes two distinctive targeting motifs; an N-terminal motif specific for the INSULIN RECEPTOR, and a C-terminal motif specific for the SH3 domain containing proteins. This subtype includes a hydrophobic domain which localizes it to the ENDOPLASMIC RETICULUM.
A subclass of receptor-like protein tryosine phosphatases that contain multiple extracellular immunoglobulin G-like domains and fibronectin type III-like domains. An additional memprin-A5-mu domain is found on some members of this subclass.
A subtype of non-receptor protein tyrosine phosphatases that contain two SRC HOMOLOGY DOMAINS. Mutations in the gene for protein tyrosine phosphatase, non-receptor type 11 are associated with NOONAN SYNDROME.
A subtype of non-receptor protein tyrosine phosphatase that is closely-related to PROTEIN TYROSINE PHOSPHATASE, NON-RECEPTOR TYPE 1. Alternative splicing of the mRNA for this phosphatase results in the production at two gene products, one of which includes a C-terminal nuclear localization domain that may be involved in the transport of the protein to the CELL NUCLEUS. Although initially referred to as T-cell protein tyrosine phosphatase the expression of this subtype occurs widely.
A Src-homology domain-containing protein tyrosine phosphatase found in the CYTOSOL of hematopoietic cells. It plays a role in signal transduction by dephosphorylating signaling proteins that are activated or inactivated by PROTEIN-TYROSINE KINASES.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.
A subclass of receptor-like protein tryosine phosphatases that contain short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.
A subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.
A subcategory of protein tyrosine phosphatases that are bound to the cell membrane. They contain cytoplasmic tyrosine phosphatase domains and extracellular protein domains that may play a role in cell-cell interactions by interacting with EXTRACELLULAR MATRIX components. They are considered receptor-like proteins in that they appear to lack specific ligands.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of a N-terminal catalytic domain and a large C-terminal domain that is enriched in PROLINE, GLUTAMIC ACID, SERINE, and THREONINE residues (PEST sequences). The phosphatase subtype is ubiquitously expressed and implicated in the regulation of a variety of biological processes such as CELL MOVEMENT; CYTOKINESIS; focal adhesion disassembly; and LYMPHOCYTE ACTIVATION.
A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing five different PDZ domains, and a carboxyl-terminal phosphatase domain. In addition to playing a role as a regulator of the FAS RECEPTOR activity this subtype interacts via its PDZ and FERM domains with a variety of INTRACELLULAR SIGNALING PROTEINS and CYTOSKELETAL PROTEINS.
Oxyvanadium ions in various states of oxidation. They act primarily as ion transport inhibitors due to their inhibition of Na(+)-, K(+)-, and Ca(+)-ATPase transport systems. They also have insulin-like action, positive inotropic action on cardiac ventricular muscle, and other metabolic effects.
A subclass of receptor-like protein tryosine phosphatases that contain a short extracellular domain, a cytosolic kinase-interaction domain, and single protein tyrosine kinase domain.
A group of enzymes removing the SERINE- or THREONINE-bound phosphate groups from a wide range of phosphoproteins, including a number of enzymes which have been phosphorylated under the action of a kinase. (Enzyme Nomenclature, 1992)
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an N-terminal catalytic domain and a C-terminal PROLINE-rich domain. The phosphatase subtype is predominantly expressed in LYMPHOCYTES and plays a key role in the inhibition of downstream T-LYMPHOCYTE activation. Polymorphisms in the gene that encodes this phosphatase subtype are associated with a variety of AUTOIMMUNE DISEASES.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular RDGS-adhesion recognition motif and a single cytosolic protein tyrosine phosphate domain.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing one or more PDZ domains, and a carboxyl-terminal phosphatase domain. Expression of this phosphatase subtype has been observed in BONE MARROW; fetal LIVER; LYMPH NODES; and T LYMPHOCYTES.
An amino acid that occurs in endogenous proteins. Tyrosine phosphorylation and dephosphorylation plays a role in cellular signal transduction and possibly in cell growth control and carcinogenesis.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
A phosphoprotein phosphatase subtype that is comprised of a catalytic subunit and two different regulatory subunits. At least two genes encode isoforms of the protein phosphatase catalytic subunit, while several isoforms of regulatory subunits exist due to the presence of multiple genes and the alternative splicing of their mRNAs. Protein phosphatase 2 acts on a broad variety of cellular proteins and may play a role as a regulator of intracellular signaling processes.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. The enzyme is comprised of a catalytic subunit and regulatory subunit. Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. A large number of proteins have been shown to act as regulatory subunits for this enzyme. Many of the regulatory subunits have additional cellular functions.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
High-molecular weight glycoproteins uniquely expressed on the surface of LEUKOCYTES and their hemopoietic progenitors. They contain a cytoplasmic protein tyrosine phosphatase activity which plays a role in intracellular signaling from the CELL SURFACE RECEPTORS. The CD45 antigens occur as multiple isoforms that result from alternative mRNA splicing and differential usage of three exons.
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
Regions of AMINO ACID SEQUENCE similarity in the SRC-FAMILY TYROSINE KINASES that fold into specific functional tertiary structures. The SH1 domain is a CATALYTIC DOMAIN. SH2 and SH3 domains are protein interaction domains. SH2 usually binds PHOSPHOTYROSINE-containing proteins and SH3 interacts with CYTOSKELETAL PROTEINS.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme.
Established cell cultures that have the potential to propagate indefinitely.
A PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing one or more PDZ domains, and a carboxyl-terminal phosphatase domain. The subtype was originally identified in a cell line derived from MEGAKARYOCYTES.
This enzyme is a lymphoid-specific src family tyrosine kinase that is critical for T-cell development and activation. Lck is associated with the cytoplasmic domains of CD4, CD8 and the beta-chain of the IL-2 receptor, and is thought to be involved in the earliest steps of TCR-mediated T-cell activation.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
An isoflavonoid derived from soy products. It inhibits PROTEIN-TYROSINE KINASE and topoisomerase-II (DNA TOPOISOMERASES, TYPE II); activity and is used as an antineoplastic and antitumor agent. Experimentally, it has been shown to induce G2 PHASE arrest in human and murine cell lines and inhibits PROTEIN-TYROSINE KINASE.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
Membrane-associated tyrosine-specific kinases encoded by the c-src genes. They have an important role in cellular growth control. Truncation of carboxy-terminal residues in pp60(c-src) leads to PP60(V-SRC) which has the ability to transform cells. This kinase pp60 c-src should not be confused with csk, also known as c-src kinase.
The rate dynamics in chemical or physical systems.
A sub-class of protein tyrosine phosphatases that contain an additional phosphatase activity which cleaves phosphate ester bonds on SERINE or THREONINE residues that are located on the same protein.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
Src-family kinases that associate with T-CELL ANTIGEN RECEPTOR and phosphorylate a wide variety of intracellular signaling molecules.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Cells grown in vitro from neoplastic tissue. If they can be established as a TUMOR CELL LINE, they can be propagated in cell culture indefinitely.
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Proteins prepared by recombinant DNA technology.
The parts of a macromolecule that directly participate in its specific combination with another molecule.
An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.
An enzyme that catalyzes the conversion of L-tyrosine, tetrahydrobiopterin, and oxygen to 3,4-dihydroxy-L-phenylalanine, dihydrobiopterin, and water. EC 1.14.16.2.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.
Cell surface proteins that bind signalling molecules external to the cell with high affinity and convert this extracellular event into one or more intracellular signals that alter the behavior of the target cell (From Alberts, Molecular Biology of the Cell, 2nd ed, pp693-5). Cell surface receptors, unlike enzymes, do not chemically alter their ligands.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
CELL LINES derived from the CV-1 cell line by transformation with a replication origin defective mutant of SV40 VIRUS, which codes for wild type large T antigen (ANTIGENS, POLYOMAVIRUS TRANSFORMING). They are used for transfection and cloning. (The CV-1 cell line was derived from the kidney of an adult male African green monkey (CERCOPITHECUS AETHIOPS).)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
A specific inhibitor of phosphoserine/threonine protein phosphatase 1 and 2a. It is also a potent tumor promoter. (Thromb Res 1992;67(4):345-54 & Cancer Res 1993;53(2):239-41)
A broad category of carrier proteins that play a role in SIGNAL TRANSDUCTION. They generally contain several modular domains, each of which having its own binding activity, and act by forming complexes with other intracellular-signaling molecules. Signal-transducing adaptor proteins lack enzyme activity, however their activity can be modulated by other signal-transducing enzymes
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
A family of synthetic protein tyrosine kinase inhibitors. They selectively inhibit receptor autophosphorylation and are used to study receptor function.
A cell surface receptor for INSULIN. It comprises a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The receptor contains an intrinsic TYROSINE KINASE domain that is located within the beta subunit. Activation of the receptor by INSULIN results in numerous metabolic changes including increased uptake of GLUCOSE into the liver, muscle, and ADIPOSE TISSUE.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
A family of non-receptor, PROLINE-rich protein-tyrosine kinases.
A Janus kinase subtype that is involved in signaling from GROWTH HORMONE RECEPTORS; PROLACTIN RECEPTORS; and a variety of CYTOKINE RECEPTORS such as ERYTHROPOIETIN RECEPTORS and INTERLEUKIN RECEPTORS. Dysregulation of Janus kinase 2 due to GENETIC TRANSLOCATIONS have been associated with a variety of MYELOPROLIFERATIVE DISORDERS.
A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.
Paxillin is a signal transducing adaptor protein that localizes to FOCAL ADHESIONS via its four LIM domains. It undergoes PHOSPHORYLATION in response to integrin-mediated CELL ADHESION, and interacts with a variety of proteins including VINCULIN; FOCAL ADHESION KINASE; PROTO-ONCOGENE PROTEIN PP60(C-SRC); and PROTO-ONCOGENE PROTEIN C-CRK.
A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.
A negative regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
Adherence of cells to surfaces or to other cells.
A signal transducer and activator of transcription that mediates cellular responses to INTERLEUKIN-6 family members. STAT3 is constitutively activated in a variety of TUMORS and is a major downstream transducer for the CYTOKINE RECEPTOR GP130.
A non-receptor protein tyrosine kinase that is localized to FOCAL ADHESIONS and is a central component of integrin-mediated SIGNAL TRANSDUCTION PATHWAYS. Focal adhesion kinase 1 interacts with PAXILLIN and undergoes PHOSPHORYLATION in response to adhesion of cell surface integrins to the EXTRACELLULAR MATRIX. Phosphorylated p125FAK protein binds to a variety of SH2 DOMAIN and SH3 DOMAIN containing proteins and helps regulate CELL ADHESION and CELL MIGRATION.
A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).
Molecules on the surface of T-lymphocytes that recognize and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (ANTIGENS, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA) or gamma-delta (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA) chains.
Any of various enzymatically catalyzed post-translational modifications of PEPTIDES or PROTEINS in the cell of origin. These modifications include carboxylation; HYDROXYLATION; ACETYLATION; PHOSPHORYLATION; METHYLATION; GLYCOSYLATION; ubiquitination; oxidation; proteolysis; and crosslinking and result in changes in molecular weight and electrophoretic motility.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Immunologic method used for detecting or quantifying immunoreactive substances. The substance is identified by first immobilizing it by blotting onto a membrane and then tagging it with labeled antibodies.
A genetically heterogeneous, multifaceted disorder characterized by short stature, webbed neck, ptosis, skeletal malformations, hypertelorism, hormonal imbalance, CRYPTORCHIDISM, multiple cardiac abnormalities (most commonly including PULMONARY VALVE STENOSIS), and some degree of INTELLECTUAL DISABILITY. The phenotype bears similarities to that of TURNER SYNDROME that occurs only in females and has its basis in a 45, X karyotype abnormality. Noonan syndrome occurs in both males and females with a normal karyotype (46,XX and 46,XY). Mutations in a several genes (PTPN11, KRAS, SOS1, NF1 and RAF1) have been associated the the NS phenotype. Mutations in PTPN11 are the most common. LEOPARD SYNDROME, a disorder that has clinical features overlapping those of Noonan Syndrome, is also due to mutations in PTPN11. In addition, there is overlap with the syndrome called neurofibromatosis-Noonan syndrome due to mutations in NF1.
Inorganic or organic compounds that contain arsenic.
Lymphocytes responsible for cell-mediated immunity. Two types have been identified - cytotoxic (T-LYMPHOCYTES, CYTOTOXIC) and helper T-lymphocytes (T-LYMPHOCYTES, HELPER-INDUCER). They are formed when lymphocytes circulate through the THYMUS GLAND and differentiate to thymocytes. When exposed to an antigen, they divide rapidly and produce large numbers of new T cells sensitized to that antigen.
Linear POLYPEPTIDES that are synthesized on RIBOSOMES and may be further modified, crosslinked, cleaved, or assembled into complex proteins with several subunits. The specific sequence of AMINO ACIDS determines the shape the polypeptide will take, during PROTEIN FOLDING, and the function of the protein.
A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN.
A contactin subtype that is predominantly expressed in the CEREBELLUM; HIPPOCAMPUS; NEOCORTEX; and HYPOTHALAMUS.
Crk-associated substrate was originally identified as a highly phosphorylated 130 kDa protein that associates with ONCOGENE PROTEIN CRK and ONCOGENE PROTEIN SRC. It is a signal transducing adaptor protein that undergoes tyrosine PHOSPHORYLATION in signaling pathways that regulate CELL MIGRATION and CELL PROLIFERATION.
A Janus kinase subtype that is involved in signaling from a broad variety of CYTOKINE RECEPTORS.
Single-stranded complementary DNA synthesized from an RNA template by the action of RNA-dependent DNA polymerase. cDNA (i.e., complementary DNA, not circular DNA, not C-DNA) is used in a variety of molecular cloning experiments as well as serving as a specific hybridization probe.
A subclass of receptor-like protein tryosine phosphatases that contain heavily glycosylated and cysteine-rich extracellular regions that include fibronectin type III-like domains.
The fission of a CELL. It includes CYTOKINESIS, when the CYTOPLASM of a cell is divided, and CELL NUCLEUS DIVISION.
A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for EXTRACELLULAR SIGNAL-REGULATED MAP KINASES.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
Benzene rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
Differentiation antigens residing on mammalian leukocytes. CD stands for cluster of differentiation, which refers to groups of monoclonal antibodies that show similar reactivity with certain subpopulations of antigens of a particular lineage or differentiation stage. The subpopulations of antigens are also known by the same CD designation.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
A proline-directed serine/threonine protein kinase which mediates signal transduction from the cell surface to the nucleus. Activation of the enzyme by phosphorylation leads to its translocation into the nucleus where it acts upon specific transcription factors. p40 MAPK and p41 MAPK are isoforms.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
Hydrocarbon rings which contain two ketone moieties in any position. They can be substituted in any position except at the ketone groups.
A cell line derived from cultured tumor cells.
A dual specificity phosphatase subtype that plays a role in intracellular signal transduction by inactivating MITOGEN-ACTIVATED PROTEIN KINASES. It has specificity for P38 MITOGEN-ACTIVATED PROTEIN KINASES and JNK MITOGEN-ACTIVATED PROTEIN KINASES.
LACTAMS forming compounds with a ring size of approximately 1-3 dozen atoms.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
A CALMODULIN-dependent enzyme that catalyzes the phosphorylation of proteins. This enzyme is also sometimes dependent on CALCIUM. A wide range of proteins can act as acceptor, including VIMENTIN; SYNAPSINS; GLYCOGEN SYNTHASE; MYOSIN LIGHT CHAINS; and the MICROTUBULE-ASSOCIATED PROTEINS. (From Enzyme Nomenclature, 1992, p277)
Short sequences (generally about 10 base pairs) of DNA that are complementary to sequences of messenger RNA and allow reverse transcriptases to start copying the adjacent sequences of mRNA. Primers are used extensively in genetic and molecular biology techniques.
A non-receptor protein-tyrosine kinase that is expressed primarily in the BRAIN; OSTEOBLASTS; and LYMPHOID CELLS. In the CENTRAL NERVOUS SYSTEM focal adhesion kinase 2 modulates ION CHANNEL function and MITOGEN-ACTIVATED PROTEIN KINASES activity.
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
An autosomal dominant disorder with an acronym of its seven features (LENTIGO; ELECTROCARDIOGRAM abnormalities; ocular HYPERTELORISM; PULMONARY STENOSIS; abnormal genitalia; retardation of growth; and DEAFNESS or SENSORINEURAL HEARING LOSS). This syndrome is caused by mutations of PTPN11 gene encoding the non-receptor PROTEIN TYROSINE PHOSPHATASE, type 11, and is an allelic to NOONAN SYNDROME. Features of LEOPARD syndrome overlap with those of NEUROFIBROMATOSIS 1 which is caused by mutations in the NEUROFIBROMATOSIS 1 GENES.
Connective tissue cells which secrete an extracellular matrix rich in collagen and other macromolecules.
The sum of the weight of all the atoms in a molecule.
A 44-kDa extracellular signal-regulated MAP kinase that may play a role the initiation and regulation of MEIOSIS; MITOSIS; and postmitotic functions in differentiated cells. It phosphorylates a number of TRANSCRIPTION FACTORS; and MICROTUBULE-ASSOCIATED PROTEINS.
Inorganic compounds that contain vanadium as an integral part of the molecule.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
A ubiquitously expressed membrane glycoprotein. It interacts with a variety of INTEGRINS and mediates responses to EXTRACELLULAR MATRIX PROTEINS.
A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form.
A member of the immunoglobulin superfamily of neuronal cell adhesion molecules that is required for proper nervous system development. Neural cell adhesion molecule L1 consists of six Ig domains, five fibronectin domains, a transmembrane region and an intracellular domain. Two splicing variants are known: a neuronal form that contains a four-amino acid RSLE sequence in the cytoplasmic domain, and a non-neuronal form that lacks the RSLE sequence. Mutations in the L1 gene result in L1 disease. Neural cell adhesion molecule L1 is predominantly expressed during development in neurons and Schwann cells; involved in cell adhesion, neuronal migration, axonal growth and pathfinding, and myelination.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
A genus of gram-negative, facultatively anaerobic rod- to coccobacillus-shaped bacteria that occurs in a broad spectrum of habitats.
Antibodies directed against immunogen-coupled phosphorylated PEPTIDES corresponding to amino acids surrounding the PHOSPHORYLATION site. They are used to study proteins involved in SIGNAL TRANSDUCTION pathways. (From Methods Mol Biol 2000; 99:177-89)
A strong oxidizing agent used in aqueous solution as a ripening agent, bleach, and topical anti-infective. It is relatively unstable and solutions deteriorate over time unless stabilized by the addition of acetanilide or similar organic materials.
A basic element found in nearly all organized tissues. It is a member of the alkaline earth family of metals with the atomic symbol Ca, atomic number 20, and atomic weight 40. Calcium is the most abundant mineral in the body and combines with phosphorus to form calcium phosphate in the bones and teeth. It is essential for the normal functioning of nerves and muscles and plays a role in blood coagulation (as factor IV) and in many enzymatic processes.
The arrangement of two or more amino acid or base sequences from an organism or organisms in such a way as to align areas of the sequences sharing common properties. The degree of relatedness or homology between the sequences is predicted computationally or statistically based on weights assigned to the elements aligned between the sequences. This in turn can serve as a potential indicator of the genetic relatedness between the organisms.
Agents that inhibit PROTEIN KINASES.
Cell surface molecules on cells of the immune system that specifically bind surface molecules or messenger molecules and trigger changes in the behavior of cells. Although these receptors were first identified in the immune system, many have important functions elsewhere.
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
Surface ligands, usually glycoproteins, that mediate cell-to-cell adhesion. Their functions include the assembly and interconnection of various vertebrate systems, as well as maintenance of tissue integration, wound healing, morphogenic movements, cellular migrations, and metastasis.
Transport proteins that carry specific substances in the blood or across cell membranes.
The part of a cell that contains the CYTOSOL and small structures excluding the CELL NUCLEUS; MITOCHONDRIA; and large VACUOLES. (Glick, Glossary of Biochemistry and Molecular Biology, 1990)
3-Phenylchromones. Isomeric form of FLAVONOIDS in which the benzene group is attached to the 3 position of the benzopyran ring instead of the 2 position.
A non-essential amino acid occurring in natural form as the L-isomer. It is synthesized from GLYCINE or THREONINE. It is involved in the biosynthesis of PURINES; PYRIMIDINES; and other amino acids.
A protein tyrosine kinase that is required for T-CELL development and T-CELL ANTIGEN RECEPTOR function.
A 51-amino acid pancreatic hormone that plays a major role in the regulation of glucose metabolism, directly by suppressing endogenous glucose production (GLYCOGENOLYSIS; GLUCONEOGENESIS) and indirectly by suppressing GLUCAGON secretion and LIPOLYSIS. Native insulin is a globular protein comprised of a zinc-coordinated hexamer. Each insulin monomer containing two chains, A (21 residues) and B (30 residues), linked by two disulfide bonds. Insulin is used as a drug to control insulin-dependent diabetes mellitus (DIABETES MELLITUS, TYPE 1).
IMMUNOGLOBULINS on the surface of B-LYMPHOCYTES. Their MESSENGER RNA contains an EXON with a membrane spanning sequence, producing immunoglobulins in the form of type I transmembrane proteins as opposed to secreted immunoglobulins (ANTIBODIES) which do not contain the membrane spanning segment.
A strain of albino rat used widely for experimental purposes because of its calmness and ease of handling. It was developed by the Sprague-Dawley Animal Company.
The relationship between the dose of an administered drug and the response of the organism to the drug.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
A signal transducer and activator of transcription that mediates cellular responses to INTERFERONS. Stat1 interacts with P53 TUMOR SUPPRESSOR PROTEIN and regulates expression of GENES involved in growth control and APOPTOSIS.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
Physiologically inactive substances that can be converted to active enzymes.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
Elements of limited time intervals, contributing to particular results or situations.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A family of immunoglobulin-related cell adhesion molecules that are involved in NERVOUS SYSTEM patterning.
The artificial induction of GENE SILENCING by the use of RNA INTERFERENCE to reduce the expression of a specific gene. It includes the use of DOUBLE-STRANDED RNA, such as SMALL INTERFERING RNA and RNA containing HAIRPIN LOOP SEQUENCE, and ANTI-SENSE OLIGONUCLEOTIDES.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Specific receptors on cell membranes that react with PLATELET-DERIVED GROWTH FACTOR, its analogs, or antagonists. The alpha PDGF receptor (RECEPTOR, PLATELET-DERIVED GROWTH FACTOR ALPHA) and the beta PDGF receptor (RECEPTOR, PLATELET-DERIVED GROWTH FACTOR BETA) are the two principle types of PDGF receptors. Activation of the protein-tyrosine kinase activity of the receptors occurs by ligand-induced dimerization or heterodimerization of PDGF receptor types.
Antigens expressed primarily on the membranes of living cells during sequential stages of maturation and differentiation. As immunologic markers they have high organ and tissue specificity and are useful as probes in studies of normal cell development as well as neoplastic transformation.
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
A mitogen-activated protein kinase subfamily that is widely expressed and plays a role in regulation of MEIOSIS; MITOSIS; and post mitotic functions in differentiated cells. The extracellular signal regulated MAP kinases are regulated by a broad variety of CELL SURFACE RECEPTORS and can be activated by certain CARCINOGENS.
Mice bearing mutant genes which are phenotypically expressed in the animals.
A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
An intracellular signaling system involving the MAP kinase cascades (three-membered protein kinase cascades). Various upstream activators, which act in response to extracellular stimuli, trigger the cascades by activating the first member of a cascade, MAP KINASE KINASE KINASES; (MAPKKKs). Activated MAPKKKs phosphorylate MITOGEN-ACTIVATED PROTEIN KINASE KINASES which in turn phosphorylate the MITOGEN-ACTIVATED PROTEIN KINASES; (MAPKs). The MAPKs then act on various downstream targets to affect gene expression. In mammals, there are several distinct MAP kinase pathways including the ERK (extracellular signal-regulated kinase) pathway, the SAPK/JNK (stress-activated protein kinase/c-jun kinase) pathway, and the p38 kinase pathway. There is some sharing of components among the pathways depending on which stimulus originates activation of the cascade.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
A phosphoprotein phosphatase that is specific for MYOSIN LIGHT CHAINS. It is composed of three subunits, which include a catalytic subunit, a myosin binding subunit, and a third subunit of unknown function.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
A lipid phosphatase that acts on phosphatidylinositol-3,4,5-trisphosphate to regulate various SIGNAL TRANSDUCTION PATHWAYS. It modulates CELL GROWTH PROCESSES; CELL MIGRATION; and APOPTOSIS. Mutations in PTEN are associated with COWDEN DISEASE and PROTEUS SYNDROME as well as NEOPLASTIC CELL TRANSFORMATION.
One of the mechanisms by which CELL DEATH occurs (compare with NECROSIS and AUTOPHAGOCYTOSIS). Apoptosis is the mechanism responsible for the physiological deletion of cells and appears to be intrinsically programmed. It is characterized by distinctive morphologic changes in the nucleus and cytoplasm, chromatin cleavage at regularly spaced sites, and the endonucleolytic cleavage of genomic DNA; (DNA FRAGMENTATION); at internucleosomal sites. This mode of cell death serves as a balance to mitosis in regulating the size of animal tissues and in mediating pathologic processes associated with tumor growth.
Chemically stimulated aggregation of cell surface receptors, which potentiates the action of the effector cell.
A family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.
A negative regulator of the CELL CYCLE that undergoes PHOSPHORYLATION by CYCLIN-DEPENDENT KINASES. RBL2 contains a conserved pocket region that binds E2F4 TRANSCRIPTION FACTOR and E2F5 TRANSCRIPTION FACTOR. RBL2 also interacts with viral ONCOPROTEINS such as POLYOMAVIRUS TUMOR ANTIGENS; ADENOVIRUS E1A PROTEINS; and PAPILLOMAVIRUS E7 PROTEINS.
Organic compounds that contain phosphorus as an integral part of the molecule. Included under this heading is broad array of synthetic compounds that are used as PESTICIDES and DRUGS.
Compounds of the general formula R-O-R arranged in a ring or crown formation.
In tissue culture, hairlike projections of neurons stimulated by growth factors and other molecules. These projections may go on to form a branched tree of dendrites or a single axon or they may be reabsorbed at a later stage of development. "Neurite" may refer to any filamentous or pointed outgrowth of an embryonal or tissue-culture neural cell.
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
The phosphoric acid ester of serine.
Morphologic alteration of small B LYMPHOCYTES or T LYMPHOCYTES in culture into large blast-like cells able to synthesize DNA and RNA and to divide mitotically. It is induced by INTERLEUKINS; MITOGENS such as PHYTOHEMAGGLUTININS, and by specific ANTIGENS. It may also occur in vivo as in GRAFT REJECTION.
A group of antigens that includes both the major and minor histocompatibility antigens. The former are genetically determined by the major histocompatibility complex. They determine tissue type for transplantation and cause allograft rejections. The latter are systems of allelic alloantigens that can cause weak transplant rejection.
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.
An serine-threonine protein kinase that requires the presence of physiological concentrations of CALCIUM and membrane PHOSPHOLIPIDS. The additional presence of DIACYLGLYCEROLS markedly increases its sensitivity to both calcium and phospholipids. The sensitivity of the enzyme can also be increased by PHORBOL ESTERS and it is believed that protein kinase C is the receptor protein of tumor-promoting phorbol esters.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Proteins that control the CELL DIVISION CYCLE. This family of proteins includes a wide variety of classes, including CYCLIN-DEPENDENT KINASES, mitogen-activated kinases, CYCLINS, and PHOSPHOPROTEIN PHOSPHATASES as well as their putative substrates such as chromatin-associated proteins, CYTOSKELETAL PROTEINS, and TRANSCRIPTION FACTORS.
Eukaryotic cell line obtained in a quiescent or stationary phase which undergoes conversion to a state of unregulated growth in culture, resembling an in vitro tumor. It occurs spontaneously or through interaction with viruses, oncogenes, radiation, or drugs/chemicals.

Activation of Src in human breast tumor cell lines: elevated levels of phosphotyrosine phosphatase activity that preferentially recognizes the Src carboxy terminal negative regulatory tyrosine 530. (1/4408)

Elevated levels of Src kinase activity have been reported in a number of human cancers, including colon and breast cancer. We have analysed four human breast tumor cell lines that exhibit high levels of Src kinase activity, and have determined that these cell lines also exhibit a high level of a phosphotyrosine phosphatase activity that recognizes the Src carboxy-terminal P-Tyr530 negative regulatory site. Total Src kinase activity in these cell lines is elevated as much as 30-fold over activity in normal control cells and specific activity is elevated as much as 5.6-fold. When the breast tumor cells were grown in the presence of the tyrosine phosphatase inhibitor vanadate, Src kinase activity was reduced in all four breast tumor cell lines, suggesting that Src was being activated by a phosphatase which could recognize the Tyr530 negative regulatory site. In fractionated cell extracts from the breast tumor cells, we found elevated levels of a membrane associated tyrosine phosphatase activity that preferentially dephosphorylated a Src family carboxy-terminal phosphopeptide containing the regulatory tyrosine 530 site. Src was hypophosphorylated in vivo at tyrosine 530 in at least two of the tumor cell lines, further suggesting that Src was being activated by a phosphatase in these cells. In preliminary immunoprecipitation and antibody depletion experiments, we were unable to correlate the major portion of this phosphatase activity with several known phosphatases.  (+info)

All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity. (2/4408)

Jun N-terminal kinases (JNKs) are serine-threonine kinases that play a critical role in the regulation of cell growth and differentiation. We previously observed that JNK activity is suppressed by all-trans-retinoic acid (t-RA), a ligand for retinoic acid nuclear receptors (RARs), in normal human bronchial epithelial cells, which are growth inhibited by t-RA. In this study, we investigated the mechanism by which t-RA inhibits JNK and the possibility that this signaling event is blocked in non-small cell lung cancer (NSCLC) cells. Virtually all NSCLC cell lines are resistant to the growth-inhibitory effects of t-RA, and a subset of them have a transcriptional defect specific to retinoid nuclear receptors. We found that in NSCLC cells expressing functional retinoid receptors, serum-induced JNK phosphorylation and activity were inhibited by t-RA in a bimodal pattern, transiently within 30 min and in a sustained fashion beginning at 12 h. Retinoid receptor transcriptional activation was required for the late, but not the early, suppression of JNK activity. t-RA inhibited serum-induced JNK activity by blocking mitogen-activated protein (MAP) kinase kinase 4-induced signaling events. This effect of t-RA was phosphatase dependent and involved an increase in the expression of the dual-specificity MAP kinase phosphatase 1 (MKP-1). t-RA did not activate MKP-1 expression or inhibit JNK activity in a NSCLC cell line with retinoid receptors that are refractory to ligand-induced transcriptional activation. These findings provide the first evidence that t-RA suppresses JNK activity by inhibiting JNK phosphorylation. Retinoid receptor transcriptional activation was necessary for the sustained inhibition of JNK activity by t-RA, and this signaling event was disrupted in NSCLC cells with retinoid receptors that are refractory to ligand-induced transcriptional activation.  (+info)

Shp-2 tyrosine phosphatase functions as a negative regulator of the interferon-stimulated Jak/STAT pathway. (3/4408)

Shp-2 is an SH2 domain-containing protein tyrosine phosphatase. Although the mechanism remains to be defined, substantial experimental data suggest that Shp-2 is primarily a positive regulator in cell growth and development. We present evidence here that Shp-2, while acting to promote mitogenic signals, also functions as a negative effector in interferon (IFN)-induced growth-inhibitory and apoptotic pathways. Treatment of mouse fibroblast cells lacking a functional Shp-2 with IFN-alpha or IFN-gamma resulted in an augmented suppression of cell viability compared to that of wild-type cells. To dissect the molecular mechanism, we examined IFN-induced activation of signal transducers and activators of transcription (STATs) by electrophoretic mobility shift assay, using a specific DNA probe (hSIE). The amounts of STAT proteins bound to hSIE upon IFN-alpha or IFN-gamma stimulation were significantly increased in Shp-2(-/-) cells. Consistently, tyrosine phosphorylation levels of Stat1 upon IFN-gamma treatment and, to a lesser extent, upon IFN-alpha stimulation were markedly elevated in mutant cells. Furthermore, IFN-gamma induced a higher level of caspase 1 expression in Shp-2(-/-) cells than in wild-type cells. Reintroduction of wild-type Shp-2 protein reversed the hypersensitivity of Shp-2(-/-) fibroblasts to the cytotoxic effect of IFN-alpha and IFN-gamma. Excessive activation of STATs by IFNs was also diminished in mutant cells in which Shp-2 had been reintroduced. Together, these results establish that Shp-2 functions as a negative regulator of the Jak/STAT pathway. We propose that Shp-2 acts to promote cell growth and survival through two mechanisms, i.e., the stimulation of growth factor-initiated mitogenic pathways and the suppression of cytotoxic effect elicited by cytokines, such as IFNs.  (+info)

Differential expression and translocation of protein tyrosine phosphatase 1B-related proteins in ME-180 tumor cells expressing apoptotic sensitivity and resistance to tumor necrosis factor: potential interaction with epidermal growth factor receptor. (4/4408)

Tumor necrosis factor (TNF)-induced apoptosis can be inhibited by overexpression of specific tyrosine kinases or activation of tyrosine kinase cascades, suggesting potential antagonism between apoptotic and tyrosine kinase signaling processes. In this report, the effects of TNF on EGF receptor tyrosine phosphorylation in ME-180 cell variants selected for apoptotic sensitivity (Sen) or resistance (Res) to TNF, previously shown to differentially express EGFr, were examined. Prior to the onset of apoptosis, TNF caused a significant reduction in the level of EGFr tyrosine phosphorylation in Sen cells but mediated only limited suppression of EGFr tyrosine phosphorylation in apoptotically resistant Res cells. In vitro incubation of cellular membranes with TNF derived from Sen cells stimulated a resident protein tyrosine phosphatase (PTP) activity which was able to dephosphorylate EGFr or tyrosine phosphopeptides mimicking an EGFr autophosphorylation site. In membrane preparations, PTPIB complexed with tyrosine phosphorylated EGFr and this association was disrupted by TNF through an apparent stimulation of PTP activity and turnover of phosphotyrosine. Intrinsic enzymatic activity of PTP1B was 2-3-fold higher in Sen versus Res cell lysates and a family of PTP1B-related proteins with altered C-termini was found to be highly expressed in Sen cells but absent or expressed at reduced levels in Res cells. Cytoplasmic extracts of Sen cells contained PTP1B-like proteins and TNF incubation resulted in the time dependent accumulation of PTP1B-like proteins in Sen cells but did not effect these proteins in Res cells. Together, these results suggest that specific changes in expression and subcellular distribution of phosphotyrosine modulatory proteins may play a role in conveying intrinsic apoptotic sensitivity to TNF in some tumor cell types.  (+info)

gp49B1 inhibits IgE-initiated mast cell activation through both immunoreceptor tyrosine-based inhibitory motifs, recruitment of src homology 2 domain-containing phosphatase-1, and suppression of early and late calcium mobilization. (5/4408)

We define by molecular, pharmacologic, and physiologic approaches the proximal mechanism by which the immunoglobulin superfamily member gp49B1 inhibits mast cell activation mediated by the high affinity Fc receptor for IgE (FcepsilonRI). In rat basophilic leukemia-2H3 cells expressing transfected mouse gp49B1, mutation of tyrosine to phenylalanine in either of the two immunoreceptor tyrosine-based inhibitory motifs of the gp49B1 cytoplasmic domain partially suppressed gp49B1-mediated inhibition of exocytosis, whereas mutation of both abolished inhibitory capacity. Sodium pervanadate elicited tyrosine phosphorylation of native gp49B1 and association of the tyrosine phosphatases src homology 2 domain-containing phosphatase-1 (SHP-1) and SHP-2 in mouse bone marrow-derived mast cells (mBMMCs). SHP-1 associated transiently with gp49B1 within 1 min after coligation of gp49B1 with cross-linked FcepsilonRI in mBMMCs. SHP-1-deficient mBMMCs exhibited a partial loss of gp49B1-mediated inhibition of FcepsilonRI-induced exocytosis at concentrations of IgE providing optimal exocytosis, revealing a central, but not exclusive, SHP-1 requirement in the counter-regulatory pathway. Coligation of gp49B1 with cross-linked FcepsilonRI on mBMMCs inhibited early release of calcium from intracellular stores and subsequent influx of extracellular calcium, consistent with SHP-1 participation. Because exocytosis is complete within 2 min in mBMMCs, our studies establish a role for SHP-1 in the initial counter-regulatory cellular responses whereby gp49B1 immunoreceptor tyrosine-based inhibition motifs rapidly transmit inhibition of FcepsilonRI-mediated exocytosis.  (+info)

Involvement of tyrosine phosphorylation in HMG-CoA reductase inhibitor-induced cell death in L6 myoblasts. (6/4408)

Our previous studies have shown that the HMG-CoA reductase (HCR) inhibitor (HCRI), simvastatin, causes myopathy in rabbits and kills L6 myoblasts. The present study was designed to elucidate the molecular mechanism of HCRI-induced cell death. We have demonstrated that simvastatin induces the tyrosine phosphorylation of several cellular proteins within 10 min. These phosphorylations were followed by apoptosis, as evidenced by the occurrence of internucleosomal DNA fragmentation and by morphological changes detected with Nomarski optics. Simvastatin-induced cell death was prevented by tyrosine kinase inhibitors. The MTT assay revealed that the addition of mevalonic acid into the culture medium partially inhibited simvastatin-induced cell death. Thus, these results suggested that protein tyrosine phosphorylation might play an important role in the intracellular signal transduction pathway mediating the HCRI-induced death of myoblasts.  (+info)

Inhibitory sites in enzymes: zinc removal and reactivation by thionein. (7/4408)

Thionein (T) has not been isolated previously from biological material. However, it is generated transiently in situ by removal of zinc from metallothionein under oxidoreductive conditions, particularly in the presence of selenium compounds. T very rapidly activates a group of enzymes in which zinc is bound at an inhibitory site. The reaction is selective, as is apparent from the fact that T does not remove zinc from the catalytic sites of zinc metalloenzymes. T instantaneously reverses the zinc inhibition with a stoichiometry commensurate with its known capacity to bind seven zinc atoms in the form of clusters in metallothionein. The zinc inhibition is much more pronounced than was previously reported, with dissociation constants in the low nanomolar range. Thus, T is an effective, endogenous chelating agent, suggesting the existence of a hitherto unknown and unrecognized biological regulatory system. T removes the metal from an inhibitory zinc-specific enzymatic site with a resultant marked increase of activity. The potential significance of this system is supported by the demonstration of its operations in enzymes involved in glycolysis and signal transduction.  (+info)

Increased insulin sensitivity and obesity resistance in mice lacking the protein tyrosine phosphatase-1B gene. (8/4408)

Protein tyrosine phosphatase-1B (PTP-1B) has been implicated in the negative regulation of insulin signaling. Disruption of the mouse homolog of the gene encoding PTP-1B yielded healthy mice that, in the fed state, had blood glucose concentrations that were slightly lower and concentrations of circulating insulin that were one-half those of their PTP-1B+/+ littermates. The enhanced insulin sensitivity of the PTP-1B-/- mice was also evident in glucose and insulin tolerance tests. The PTP-1B-/- mice showed increased phosphorylation of the insulin receptor in liver and muscle tissue after insulin injection in comparison to PTP-1B+/+ mice. On a high-fat diet, the PTP-1B-/- and PTP-1B+/- mice were resistant to weight gain and remained insulin sensitive, whereas the PTP-1B+/+ mice rapidly gained weight and became insulin resistant. These results demonstrate that PTP-1B has a major role in modulating both insulin sensitivity and fuel metabolism, thereby establishing it as a potential therapeutic target in the treatment of type 2 diabetes and obesity.  (+info)

BioAssay record AID 743310 submitted by Burnham Center for Chemical Genomics: SAR confirmation of uHTS small molecule inhibitors of Low Molecular Weight Protein Tyrosine Phosphatase, LMPTP, in a fluorescence-based, VHR-1 (dual specificity phosphatase 3) selectivity assay.
Vanadium in PDB 5jnw: Crystal Structure of Bovine Low Molecular Weight Protein Tyrosine Phosphatase (Lmptp) Mutant (W49Y N50E) Complexed with Vanadate and Uncompetitive Inhibitor
Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology. Uppsala University, Teknisk-naturvetenskapliga vetenskapsområdet, Faculty of Science and Technology, Biology, Department of Cell and Molecular Biology, Structural Molecular Biology. ...
TY - JOUR. T1 - Receptor protein tyrosine phosphatases are novel components of a polycystin complex. AU - Boucher, Catherine A.. AU - Ward, Heather H.. AU - Case, Ruth L.. AU - Thurston, Katie S.. AU - Li, Xiaohong. AU - Needham, Andrew. AU - Romero, Elsa. AU - Hyink, Deborah. AU - Qamar, Seema. AU - Roitbak, Tamara. AU - Powell, Samantha. AU - Ward, Christopher. AU - Wilson, Patricia D.. AU - Wandinger-Ness, Angela. AU - Sandford, Richard N.. N1 - Funding Information: This work was supported by grants from The National Kidney Research Fund (now Kidney Research UK) , The Wellcome Trust, NIDDK ( R01 DK50141 ), PKD Foundation ( 12(A-C)2R ) and NIH ( DK P0162345 ). RS is a former Wellcome Trust Senior Fellow in Clinical Research. KST was a Wellcome Trust Prize Student. TR (F758) and HHW (552883) were supported by National Kidney Foundation Fellowships. Cell lines were the kind gifts of multiple individuals: A431 cells from Dr. Folma Buss, University of Cambridge; IMCD3 cells from Dr. John H. ...
TY - JOUR. T1 - Receptor-associated constitutive protein tyrosine phosphatase activity controls the kinase function of JAK1. AU - Haque, S. Jaharul. AU - Wu, Qian. AU - Kammer, Winfried. AU - Friedrich, Karlheinz. AU - Smith, Jonathan M.. AU - Kerr, Ian M.. AU - Stark, George R.. AU - Williams, Bryan R.G.. PY - 1997/8/5. Y1 - 1997/8/5. N2 - Exposure of cells to protein tyrosine phosphatase (PTP) inhibitors causes an increase in the phosphotyrosine content of many cellular proteins. However, the level at which the primary signaling event is affected is still unclear. We show that Jaks are activated by tyrosine phosphorylation in cells that are briefly exposed to the PTP inhibitor pervanadate (PV), resulting in tyrosine phosphorylation and functional activation of Stat6 (in addition to other Stats). Mutant cell lines that lack Jak1 activity fail to support PV- mediated [or interleukin 4 (IL-4)-dependent] activation of Stat6 but can be rescued by complementation with functional Jak1. The docking ...
Lenti ORF particles, PPFIA1 (mGFP-tagged) - Human protein tyrosine phosphatase, receptor type, f polypeptide (PTPRF), interacting protein (liprin), alpha 1 (PPFIA1), transcript variant 1, 200 uL, |10^7 TU/mL, 200 µl.
Abstract: Low molecular weight protein tyrosine phosphatases (LMW-PTPs) are small enzymes that are ubiquitous in many organisms. They are important in biological processes such as cell proliferation, adhesion, migration, and invasiveness. LMW-PTP is expressed in mammalian cells as two isoforms (IF1 and IF2) originating through alternative splicing. We have previously shown that IF2 targets lipid rafts called caveolae and interacts with caveolin-1, their major structural protein. Caveolae are cholesterol- and sphingolipid-rich membrane microdomains that have been implicated in a variety of cellular functions, including signal transduction events. Caveolin-1 contains a scaffolding region that contributes to the binding of the protein to the plasma membrane and mediates protein omo- and etero-oligomerization. Interaction of many signaling molecules with the scaffolding domain sequesters them into caveolae and inhibits or suppresses their activities. Caveolin-interacting proteins usually have a ...
Sui, X., Hyun, S. W., Kiser, T. D., Del Vecchio, R. L., Tonks, N. K., Passaniti, A., Goldblum, S. E. (November 2004) Receptor protein tyrosine phosphatase (PTP) mu regulates the endothelial paracellular pathway. Molecular Biology of the Cell, 15. 428A-428A. ISSN 1059-1524 ...
Title:Inhibitor Binding Sites in the Protein Tyrosine Phosphatase SHP-2. VOLUME: 20 ISSUE: 11. Author(s):Haonan Zhang, Zhengquan Gao, Chunxiao Meng*, Xiangqian Li* and Dayong Shi*. Affiliation:School of Life Sciences, Shandong University of Technology, Zibo 255049, Shandong Province, School of Life Sciences, Shandong University of Technology, Zibo 255049, Shandong Province, School of Life Sciences, Shandong University of Technology, Zibo 255049, Shandong Province, State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, Shandong, State Key Laboratory of Microbial Technology, Shandong University, Jinan, 250100, Shandong. Keywords:PTP, SHP-2, SHP-1, protein tyrosine kinases, PTKs, cancer.. Abstract:Protein tyrosine phosphatase 2 (SHP-2) has long been proposed as a cancer drug target. Several small-molecule compounds with different mechanisms of SHP-2 inhibition have been reported, but none are commercially available. Pool selectivity over protein tyrosine phosphatase 1 ...
Protein tyrosine phosphatase type IVA 3 is an enzyme belongs to a small class of prenylated protein tyrosine phosphatases (PTPs). PTPs are cell signaling molecules that play regulatory roles in a variety of cellular processes. This class of PTPs contain a PTP domain and a characteristic C-terminal prenylation motif. Studies of this class of PTPs in mice demonstrated that they were prenylated proteins in vivo, which suggested their association with cell plasma membrane. Overexpression of this gene in mammalian cells was reported to inhibit angiotensin-II induced cell calcium mobilization and promote cell growth. Two alternatively spliced variants exist.Mainly expressed in cardiomyocytes and skeletal muscle; also found in pancreas. Consistently overexpressed in colon cancer metastasis.
1JL3: Bacillus subtilis arsenate reductase is structurally and functionally similar to low molecular weight protein tyrosine phosphatases.
TY - JOUR. T1 - Enhancement or induction of neurite formation by a protein tyrosine phosphatase inhibitor, 3,4-dephostatin, in growth factor-treated PC12h cells. AU - Fujiwara, Sari. AU - Watanabe, Takumi. AU - Nagatsu, Toshiharu. AU - Gohda, Jin. AU - Imoto, Masaya. AU - Umezawa, Kazuo. PY - 1997/9/8. Y1 - 1997/9/8. N2 - We studied the effect of the 3,4 dihydroxy analogue of dephostatin (3,4-dephostatin), an inhibitor of protein-tyrosine phosphatase (PTPase), on the differentiation of rat pheochromocytoma PC12 cells. 3,4-Dephostatin accelerated NGF-induced neurite formation in PC12h cells, a subline of PC12 cells, whereas the inhibitor alone did not induce neurite formation. It sustained the NGF-induced tyrosine phosphorylation of several proteins, most prominently that of mitogen-activated protein (MAP) kinase. EGF alone did not induce differentiation in PC12h cells, but it induced neurite formation in the presence of 3,4-dephostatin. The inhibitor also prolonged EGF-induced tyrosine ...
TY - JOUR. T1 - Purification and characterization of a protein tyrosine phosphatase which dephosphorylates the nicotinic acetylcholine receptor. AU - Mei, Lin. AU - Huganir, Richard L.. PY - 1991/12/1. Y1 - 1991/12/1. N2 - The nicotinic acetylcholine receptor (nAChR) is phosphorylated to a high stoichiometry on tyrosine residues both in vitro and in vivo. Moreover, tyrosine phosphorylation has been shown to regulate the functional properties of the receptor. We report here the purification and characterization of a protein tyrosine phosphatase that dephosphorylates tyrosine-phosphorylated nAChR from Torpedo electroplax, a tissue highly enriched in the nAChR. The 32P-labeled tyrosine phosphorylated nAChR was used as a substrate to monitor the enzyme activity during purification. The protein tyrosine phosphatase activity was purified using three consecutive cation-exchange columns (phosphocellulose, S Sepharose Fast Flow, Bio-Rex 70), followed by two affinity matrices (p-aminobenzylphosphonic ...
Protein tyrosine phosphatase (PTP) Shp2 is a non-receptor PTP that involved in cell signaling and regulation of cell proliferation, differentiation, and migration. Shp2 mediates activation of kinases that are involved in the pathogenesis of human carcinoma. NSC-117199 was identified as a porent inhibitor of the protein tyrosine phosphatase (PTPa) Shp2. A focused library of analogs incorporating an isatin scaffold was designed and evaluated for inhibition of Shp2 and Shp1 PTP activities. Several compounds were identified that selectively inhibit Shp2 over Shp1 and PTP1B with low to sub-micromolar activity. Also disclosed are methods of inhibiting a protein tyrosine phosphatase in a cell and treating cancer through selective inhibition of Shp2.
Site-directed mutagenesis of a synthetic gene coding for low-M(r) phosphotyrosine protein phosphatase from bovine liver has been carried out. The two histidine residues in the enzyme have been mutated to glutamine; both single and double mutants were produced. The mutated and non-mutated sequences have been expressed in Escherichia coli as fusion proteins, in which the low-M(r) phosphotyrosine protein phosphatase was linked to the C-terminal end of the maltose-binding protein. The fusion enzymes were easily purified by single-step affinity chromatography. The mutants were studied for their kinetic properties. Both single mutants showed decreased kcat. values (30 and 7% residual activities for His66 and His72 respectively), and alterations of the Ki values relative to four-competitive inhibitors were observed. The kinetic mechanism of p-nitrophenyl phosphate hydrolysis in the presence of both single mutants was determined and compared with that of the non-mutated enzyme. The rate-determining step ...
TY - JOUR. T1 - Investigating Mammalian Tyrosine Phosphatase Inhibitors as Potential Piggyback Leads to Target Trypanosoma brucei Transmission. AU - Ruberto, Irene. AU - Szoor, Balazs. AU - Clark, Rachel. AU - Matthews, Keith R.. PY - 2013/2. Y1 - 2013/2. N2 - African trypanosomiasis is a neglected tropical disease affecting humans and animals across 36 sub-Saharan African countries. We have investigated the potential to exploit a piggyback approach to inhibit Trypanosoma brucei transmission by targeting the key developmental regulator of transmission, T. brucei protein tyrosine phosphatase 1. This strategy took advantage of the extensive investment in inhibitors for human protein tyrosine phosphatase 1B, a key target for pharmaceutical companies for the treatment of obesity and diabetes. Structural predictions for human and trypanosome tyrosine phosphatases revealed the overall conservation of important functional motifs, validating the potential for exploiting cross specific compounds. ...
TY - JOUR. T1 - Hepatic tyrosine-phosphorylated proteins identified and localized following in vivo inhibition of protein tyrosine phosphatases. T2 - effects of H2O2 and vanadate administration into rat livers. AU - Hadari, Yaron R.. AU - Geiger, Benjamin. AU - Nadiv, Orna. AU - Sabanay, Ilana. AU - Roberts, Charles T.. AU - LeRoith, Derek. AU - Zick, Yehiel. PY - 1993/11. Y1 - 1993/11. N2 - Injection of a combination of H2O2 and vanadate (H/V) into the portal vein of rat livers resulted in inhibition of protein tyrosine phosphatase activity and led to a dramatic enhanced in vivo protein tyrosine phosphorylation. Some of the phosphorylated proteins were identified as the β-subunit of the insulin receptor, the insulin receptor substrate 1 (ppl85), PLC-γ (pp145), and a 100 kDa PLC-γ-associated protein. Immunofluorescense and immune electron microscopy of frozen liver sections with anti-P-Tyr antibodies revealed that most of the tyrosine-phosphorylated proteins are localized in close proximity ...
Protein tyrosine phosphatases play important role in immune function. They dephosphorylate and inactivate signals emanating from the plasma membrane to influence different processes within cells. In allergic reactions, signals triggered by the aggregation of IgE receptors expressed on the surface of mast cells are also inactivated by protein tyrosine phosphatases. As a number of these phosphatases is transcriptionally regulated by glucocorticoids, it is thought that the inhibitory effects of glucocorticoids in mast cells in allergy occur at the level of expression of protein tyrosine phosphatase genes. The long-term application of glucocorticoids is associated with several adverse reactions. A better understanding of the mode of action of glucocorticoids is therefore required to reduce the side effects. The aim of this work is to use knock-out mouse models and biochemical and molecular biological techniques to identify the mechanism by which glucocorticoid-mediated regulation of protein tyrosine ...
SIGNIFICANCE: Tyrosine phosphorylation and associated protein tyrosine phosphatases are gaining prominence as critical mechanisms in the regulation of fundamental processes in a wide variety of bacteria. In particular, these phosphatases have been associated with the control of the biosynthesis of capsular polysaccharides and extracellular polysaccharides, critically important virulence factors for bacteria.RECENT ADVANCES: Deletion and over-expression of the phosphatases result in altered polysaccharide biosynthesis in a range of bacteria. The recent structures of associated auto-phosphorylating tyrosine kinases has suggested that the phosphatases may be critical for the cycling of the kinases between monomers and higher order oligomers. CRITICAL ISSUES: Additional substrates of the phosphatases apart from cognate kinases are currently being identified. These are likely to be critical to our understanding of the mechanism by which polysaccharide biosynthesis is regulated. FUTURE DIRECTIONS: ...
Protein tyrosine phosphatases (PTPs) cooperate with protein tyrosine kinases to regulate signal transduction pathways. Genome-wide surveys cataloging protein tyrosine phosphatases in humans have recently been carried out. Here, we present a bioinformatics analysis of protein tyrosine phosphatases in the human genome to examine their domain architecture, alternative splicing and pseudogenes. We present evidence that alternative transcripts exist for 25 out of 35 PTPs analyzed. These alternative transcripts include novel exons; skipped exons as well as cryptic donor/acceptor splice sites. We discovered a novel isoform of PTPN18 based on analysis of expressed sequence tags (ESTs). The deletion of 4 exons in the catalytic domain of the novel isoform may alter the enzymatic activity toward its substrates. We were able to experimentally validate 2 of our novel isoform predictions through RT-PCR. Finally, a user-friendly web-based resource that consolidates the gene and protein annotations for all ...
TY - JOUR. T1 - Reduced protein tyrosine phosphatase (PTPase) activity of CD45 on peripheral blood lymphocytes in patients with systemic lupus erythematosus (SLE). AU - Takeuchi, T.. AU - Pang, M.. AU - Amano, K.. AU - Koide, J.. AU - Abe, T.. PY - 1997/1/1. Y1 - 1997/1/1. N2 - To disclose the mechanism of aberrant function of peripheral blood lymphocytes (PBL) in SLE, we focused on the catalytic function of CD45, and determined the CD45 PTPase activity in SLE patients. The sample population consisted of 32 SLE patients with different disease activity. PTPase activity of cell lysates immunoprecipitated by anti-CD45 MoAb was assayed against phosphotyrosine analogue PNPP, followed by measuring the release of para- nitro phenol at 410 nm. CD45 PTPase activity of PBL was significantly decreased in SLE patients, compared with that of normal controls and patients with systemic sclerosis (964 ± 265, 1202 ± 172, 1210 ± 125, respectively; SLE versus normal, P,0.05). It was correlated with SLE Disease ...
Efficient total synthesis of pulchellalactam, a CD45 protein tyrosine phosphatase inhibitor. by Wen-Ren Li, Sung Tsai Lin, Nai-Mu Hsu, Meei-Shiou Chern. The Journal of organic chemistry. Read more related scholarly scientific articles and abstracts.
TY - JOUR. T1 - The protein tyrosine phosphatase Shp-2 regulates RhoA activity. AU - Schoenwaelder, Simone M.. AU - Petch, Leslie A.. AU - Williamson, David. AU - Shen, Randy. AU - Feng, Gen Sheng. AU - Burridge, Keith. PY - 2000/11/30. Y1 - 2000/11/30. N2 - Remodeling of filamentous actin into distinct arrangements is precisely controlled by members of the Rho family of small GTPases [1]. A well characterized member of this family is RhoA, whose activation results in reorganization of the cytoskeleton into thick actin stress fibers terminating in Integrin-rich focal adhesions [2]. Regulation of RhoA is required to maintain adhesion in stationary cells, but is also critical for cell spreading and migration [3]. Despite its biological importance, the signaling events leading to RhoA activation are not fully understood. Several independent studies have implicated tyrosine phosphorylation as a critical event upstream of RhoA [4]. Consistent with this, our recent studies have demonstrated the ...
Gliomas are a diverse group of brain tumors of glial origin. Most are characterized by diffuse infiltrative growth in the surrounding brain. In combination with their refractive nature to chemotherapy this makes it almost impossible to cure patients using combinations of conventional therapeutic strategies. The drastically increased knowledge about the molecular underpinnings of gliomas during the last decade has elicited high expectations for a more rational and effective therapy for these tumors. Most studies on the molecular pathways involved in glioma biology thus far had a strong focus on growth factor receptor protein tyrosine kinase (PTK) and phosphatidylinositol phosphatase signaling pathways. Except for the tumor suppressor PTEN, much less attention has been paid to the PTK counterparts, the protein tyrosine phosphatase (PTP) superfamily, in gliomas. PTPs are instrumental in the reversible phosphorylation of tyrosine residues and have emerged as important regulators of signaling ...
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The protein tyrosine kinase (PTK) receptors and cytosolic signaling proteins as well as the protein tyrosine phosphatases (PTPs) have important roles in regulation of growth of the benign and malignant prostate gland. Here, we studied expression of the protein tyrosine phosphatase SHP-1 in prostate cancer cell lines and in human prostatic tissues. SHP-1 is expressed at a high level in LNCaP prostate cancer cells compared with PC3 cells. Silencing of SHP-1 expression with siRNA in LNCaP cells led to an increased rate of proliferation, whereas overexpression of SHP-1 by means of transient and stable transfection in PC3 cells led to a decrease in proliferation. Corresponding changes were observed in cyclin D1 expression. We further demonstrate that LNCaP and PC3 cells respond differently to IL-6 stimulation. SHP-1 overexpression in PC3 cells reversed IL-6 stimulation of proliferation, whereas in SHP-1-silenced LNCaP cells, IL-6 inhibition of proliferation was not affected. In addition, IL-6 ...
TY - JOUR. T1 - Synthesis and cell-based activity of a potent and selective protein tyrosine phosphatase 1B inhibitor prodrug. AU - Boutselis, Irene G.. AU - Yu, Xiao. AU - Zhang, Zhong-Yin. AU - Borch, Richard F.. PY - 2007/2/22. Y1 - 2007/2/22. N2 - Our laboratory recently reported the development of novel prodrug chemistry for the intracellular delivery of phosphotyrosine mimetics. This chemistry has now been adapted for the synthesis of a prodrug that delivers the nonhydrolyzable difluoromethylphosphonate moiety intracellularly. Activation of the prodrug generates a difluoromethylphosphonamidate anion that undergoes subsequent cyclization and hydrolysis with a t1/2 = 44 min. A highly potent and selective inhibitor of protein tyrosine phosphatase 1B (PTP1B) with a nanomolar Ki has been reported, but this bis(difluoromethylphosphonate) lacks potential utility due to its exceedingly low membrane permeability at physiological pH. A prodrug of this inhibitor has been synthesized and evaluated in ...
Definition of PEP protein tyrosine phosphatase with photos and pictures, translations, sample usage, and additional links for more information.
cytoplasm, protein tyrosine phosphatase activity, mitotic cell cycle, negative regulation of ERK1 and ERK2 cascade, negative regulation of Ras protein signal transduction, protein dephosphorylation, R7 cell fate commitment, Ras protein signal transduction
TY - JOUR. T1 - Therapeutic targeting of oncogenic tyrosine phosphatases. AU - Frankson, Rochelle. AU - Yu, Zhi Hong. AU - Bai, Yunpeng. AU - Li, Qinglin. AU - Zhang, Ruo Yu. AU - Zhang, Zhong Yin. PY - 2017/11/1. Y1 - 2017/11/1. N2 - Protein tyrosine phosphatases (PTP) are exciting and novel targets for cancer drug discovery that work in concert with protein tyrosine kinases (PTK) in controlling cellular homeostasis. Given the activating role that some PTKs play in initiating growth factor-mediated cellular processes, PTPs are usually perceived as the negative regulators of these events and therefore tumor suppressive in nature. However, mounting evidence indicate that PTPs do not always antagonize the activity of PTKs in regulating tyrosine phosphorylation, but can also play dominant roles in the initiation and progression of signaling cascades that regulate cell functions. It follows, therefore, that PTP malfunction can actively contribute to a host of human disorders, in particular, cancer, ...
This book provides coverage, methodology, and laboratory protocols on the more essential aspects of protein tyrosine phosphatase (PTP) function and regulation, including the use of standardized in vitro functional assays, suitable cell systems, and animal and microorganism models. Chapters covering
In contrast to receptor protein tyrosine kinases and associated downstream signaling events in the cardiovascular system, the protein tyrosine phosphatases that potentially function as counter-regulatory agents have been less extensively investigated. Thus, the present study addressed the functional role of the ubiquitous phosphatase PTP1B in cultured rat aortic smooth muscle cells and in carotid arteries. In addition to targeting the PDGF receptor, PTP1B has been reported to induce dephosphorylation of several other receptor tyrosine kinases, including the insulin receptor,17 epidermal growth factor receptor,30 and IGF-1 receptor.15. We report for the first time that PTP1B targets PDGF- or FGF-induced cell motility and proliferation in vitro and neointima formation in vivo. It is interesting to note a recent study indicating that signaling events downstream of the PDGF receptor were not significantly altered in fibroblasts genetically lacking PTP1B, although receptor tyrosyl phosphorylation ...
Cross-linking B cell antigen receptor (BCR) elicits early signal transduction events, including activation of protein tyrosine kinases, phosphorylation of receptor components, activation of phospholipase C-gamma (PLC-gamma), and increases in intracellular free Ca2+. In this article, we report that cross-linking the BCR led to a rapid translocation of cytosolic protein tyrosine phosphatase (PTP) 1C to the particulate fraction, where it became associated with a 140-150-kD tyrosyl-phosphorylated protein. Western blotting analysis identified this 140-150-kD protein to be CD22. The association of PTP-1C with CD22 was mediated by the NH2-terminal Src homology 2 (SH2) domain of PTP-1C. Complexes of either CD22/PTP-1C/Syk/PLC-gamma(1) could be isolated from B cells stimulated by BCR engagement or a mixture of hydrogen peroxidase and sodium orthovanadate, respectively. The binding of PLC-gamma(1) and Syk to tyrosyl-phosphorylated CD22 was mediated by the NH2-terminal SH2 domain of PLC-gamma(1) and the ...
The levels of tyrosine phosphorylation required for cell growth and differentiation are achieved through the coordinated action of protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). Depending upon the cellular context, these two types of enzymes may either antagonize or cooperate with each other during the signal transmission process. An imbalance between these enzymes may impair normal cell growth, leading to cellular transformation. Both PTKs and PTPs have evolved to a level of structural diversity that allows them to regulate many cellular processes. This review will focus on several specific examples that highlight the interplay between PTPs and PTKs in cell signaling.. ...
TY - JOUR. T1 - Heat shock-induced activation of stress MAP kinase is regulated by threonine-and tyrosine-specific phosphatases. AU - Nguyen, Aaron Ngocky. AU - Shiozaki, Kazuhiro. PY - 1999/7/1. Y1 - 1999/7/1. N2 - In eukaryotic species from yeast to human, stress-activated protein kinases (SAPKs), members of a MAP kinase (MAPK) subfamily, regulate the transcriptional response to various environmental stress. It is poorly understood how diverse forms of stress are sensed and transmitted to SAPKs. Here, we report the heat shock regulation of the fission yeast Spc1 SAPK, a homolog of human p38 and budding yeast Hog1p. Although osmostress and oxidative stress induce strong activation of the Wis1 MAPK kinase (MEK), which activates Spc1 through Thr-171/Tyr-173 phosphorylation, activation of Wis1 upon heat shock is relatively weak and transient. However, in heat- shocked cells, Pyp1, the major tyrosine phosphatase that dephosphorylates and inactivates Spc1, is inhibited for its interaction with Spc1, ...
Principal Investigator:HONDA Hiroaki, Project Period (FY):1995 - 1996, Research Category:Grant-in-Aid for Scientific Research (C), Section:一般, Research Field:Hematology
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing one or more PDZ domains, and a carboxyl-terminal phosphatase domain. Expression of this phosphatase subtype has been observed in BONE MARROW; fetal LIVER; LYMPH NODES; and T LYMPHOCYTES ...
With the current access to the whole genomes of various organisms and the completion of the first draft of the human genome, there is a strong need for a structure-function classification of protein families as an initial step in moving from DNA databases to a comprehensive understanding of human biology. As a result of the explosion in nucleic acid sequence information and the concurrent development of methods for high-throughput functional characterization of gene products, the genomic revolution also promises to provide a new paradigm for drug discovery, enabling the identification of molecular drug targets in a significant number of human diseases. This molecular view of diseases has contributed to the importance of combining primary sequence data with three-dimensional structure and has increased the awareness of computational homology modeling and its potential to elucidate protein function. In particular, when important proteins or novel therapeutic targets are identified-like the family ...
With more than 12 million people affected worldwide, 2 million new cases occurring per year, and the rapid emergence of drug resistance and treatment failure, leishmaniasis is an infectious disease for which research on drug and vaccine development, host-pathogen, and vector-parasite interactions are current international priorities. Upon Leishmania-macrophage interaction, activation of the protein tyrosine phosphatase (PTP) SHP-1 rapidly leads to the down-regulation of Janus kinase and mitogen-activated protein kinase signaling, resulting in the attenuation of host innate inflammatory responses and of various microbicidal macrophage functions. We report that, in addition to SHP-1, the PTPs PTP1B and TCPTP are activated and posttranslationally modified in infected macrophages, and we identify an essential role for PTP1B in the in vivo progression of Leishmania infection. The mechanism underlying PTP modulation involves the proteolytic activity of the Leishmania surface protease GP63. Access of ...
FUNCTION: [Summary is not available for the mouse gene. This summary is for the human ortholog.] The protein encoded by this gene is the founding member of the protein tyrosine phosphatase (PTP) family, which was isolated and identified based on its enzymatic activity and amino acid sequence. PTPs catalyze the hydrolysis of the phosphate monoesters specifically on tyrosine residues. Members of the PTP family share a highly conserved catalytic motif, which is essential for the catalytic activity. PTPs are known to be signaling molecules that regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. This PTP has been shown to act as a negative regulator of insulin signaling by dephosphorylating the phosphotryosine residues of insulin receptor kinase. This PTP was also reported to dephosphorylate epidermal growth factor receptor kinase, as well as JAK2 and TYK2 kinases, which implicated the role of this PTP in cell growth control, ...
Protein Tyrosine Phosphatase 1B (PTP1B) has been shown to be a negative regulator of insulin signaling by dephosphorylating key tyrosine residues within the regulatory domain of the β-subunit of the insulin receptor. Recent gene knockout studies in m
Tyrosine phosphatase inhibition with chemical agents such as vanadate rapidly triggers T cell signaling, supporting the notion that tyrosine phosphatase exclusion could be used as a trigger for tyrosine kinase cascades (29, 30). Phosphatase exclusion models for immune cell triggering typically focus on the hematopoietic phosphatase CD45, which is a type I transmembrane protein with a large extracellular domain and a cytoplasmic tyrosine phosphatase domain (31, 32). TCRs and NK cells activating receptors all utilize the Src family tyrosine kinase Lck to mediate early phosphorylation events (33, 34). CD45 maintains Lck in an active state by removing a C-terminal inhibitory phosphate. However, CD45 also deactivates several targets of Lck at antigen receptors, and thus it was proposed, first as speculation by Springer (31) and later with experimental support by van der Merwe and my group (10, 35), that CD45 exclusion is a key initial event in TCR triggering. Addressing this issue at present requires ...
TY - JOUR. T1 - Chrysin restores PDGF-induced inhibition on protein tyrosine phosphatase and reduces PDGF signaling in cultured VSMCs. AU - Lo, Huey Ming. AU - Wu, Min Wen. AU - Pan, Shiow Lin. AU - Peng, Chieh Yu. AU - Wu, Pi Hui. AU - Wu, Wen Bin. PY - 2012/6. Y1 - 2012/6. N2 - Previous studies have shown that an increased intake of dietary flavonoids is associated with a decreased risk of cardiovascular diseases (CVDs). PDGF is a major mitogen for vascular smooth muscle cell (VSMC) and participates in the pathogenesis of many CVDs. The study investigated whether the flavone chrysin affected PDGF functions in VSMCs and neointma formation in rat artery. We found that chrysin concentration-dependently inhibited PDGF-induced proliferation and chemotaxis and reduced PDGF signaling in VSMCs. Chrysin attenuated H2O2 signaling and PDGF-induced reactive oxygen species production and NADPH oxidase activation but did not interfere with PDGF binding to VSMCs. The further analyses revealed that chrysin ...
Recombinant Protein tyrosine Phosphatase Type IVA, Member 2 (PTP4A2) Protein (His tag). Species: Human. Source: Escherichia coli (E. coli). Order product ABIN667818.
Recombinant Protein tyrosine Phosphatase Type IVA, Member 2 (PTP4A2) Protein (His tag). Species: Human. Source: Insect Cells. Order product ABIN3074452.
BioAssay record AID 165316 submitted by ChEMBL: In vivo inhibitory activity against Protein tyrosine phosphatase 1B (PTP1B) over-expressed in intact Sf9 cell assay; NA denotes not active.
Smith AM, Maguire-Nguyen KK, Rando TA, Zasloff MA, Strange KB, Yin VP. The protein tyrosine phosphatase 1B inhibitor MSI-1436 stimulates regeneration of heart
TY - JOUR. T1 - Neuronal protein tyrosine phosphatase 1B deficiency results in inhibition of hypothalamic AMPK and isoform-specific activation of AMPK in peripheral tissues. AU - Xue, Bingzhong. AU - Pulinilkunnil, Thomas. AU - Murano, Incoronata. AU - Bence, Kendra K.. AU - He, Huamei. AU - Minokoshi, Yasuhiko. AU - Asakura, Kenji. AU - Lee, Anna. AU - Haj, Fawaz. AU - Furukawa, Noboru. AU - Catalano, Karyn J.. AU - Delibegovic, Mirela. AU - Balschi, James A.. AU - Cinti, Saverio. AU - Neel, Benjamin G.. AU - Kahn, Barbara B.. PY - 2009/8. Y1 - 2009/8. N2 - PTP1B-/- mice are resistant to diet-induced obesity due to leptin hypersensitivity and consequent increased energy expenditure. We aimed to determine the cellular mechanisms underlying this metabolic state. AMPK is an important mediator of leptins metabolic effects. We find that α1 and α2 AMPK activity are elevated and acetylcoenzyme A carboxylase activity is decreased in the muscle and brown adipose tissue (BAT) of PTP1B-/- mice. The ...
PubMed journal article Regulation of the insulin antagonistic protein tyrosine phosphatase 1B by dietary Se studied in growing rat were found in PRIME PubMed. Download Prime PubMed App to iPhone or iPad.
TY - THES. T1 - Functional Characterization of Protein -Tyrosine Phosphatases in Zebrafish Development using Image Analysis. AU - Runtuwene, V.J.. N1 - Reporting year: 2012. PY - 2012. Y1 - 2012. M3 - PhD thesis (Proefschrift). ER - ...
... purple acid phosphatases (PAPs), and most recently, protein tyrosine phosphatase-like phytases (PTP-like phytases). Most of the ... "Kinetic and structural analysis of a bacterial protein tyrosine phosphatase-like myo-inositol polyphosphatase". Protein Science ... Zhang ZY (2003). Mechanistic studies on protein tyrosine phosphatases. Prog. Nucleic Acid Res. Mol. Biol. Progress in Nucleic ... Puhl A, Greiner R, Selinger LB (2008). "A protein tyrosine phosphatase-like inositol polyphosphatase from Selenomonas ...
"Protein tyrosine phosphatases in the human genome". Cell. 117 (6): 699-711. doi:10.1016/j.cell.2004.05.018. PMID 15186772. ... Myotubularin related protein 14 also known as MTMR14 is a protein which in humans is encoded by the MTMR14 gene. Expression of ... MTMR14 is a phosphatidylinositol-3-phosphatase that dephosphorylates the same substrates as myotubularin, PtdIns(3)P and PtdIns ... 2000). "Systematic subcellular localization of novel proteins identified by large-scale cDNA sequencing". EMBO Rep. 1 (3): 287- ...
June 2004). "Protein tyrosine phosphatases in the human genome". Cell. 117 (6): 699-711. doi:10.1016/j.cell.2004.05.018. PMID ... The FA proteins play an elaborate role with FAN1 to remove these ICLs. The pathway consists of 15 known proteins. Three of them ... It is a structure dependent endonuclease and a member of the myotubularin-related class 1 cysteine-based protein tyrosine ... This is present in proteins that bind to ubiquitinated proteins, and is highly conserved across eukaryotes. This Zinc finger is ...
Protein Tyrosine Phosphatase; Rab11a: Member RAS Oncogene Family; RGS2: Regulator Of G-Protein Signaling 2; RyR1: Ryanodine ... "TRPV6 protein expression summary". The Human Protein Atlas. Retrieved 2020-08-01. Lehen'kyi V, Raphaël M, Prevarskaya N (March ... Shin YC, Shin SY, So I, Kwon D, Jeon JH (January 2011). "TRIP Database: a manually curated database of protein-protein ... of proteins. The TRP family is a group of channel proteins critical for ionic homeostasis and the perception of various ...
Lorenz, Ulrike (2017-05-07). "Protein Tyrosine Phosphatase Assays". Current Protocols in Immunology. 91 (1): 11.7.1-12. doi: ... This property can be used to determine the activity of various phosphatases including alkaline phosphatase (AP) and protein ... tyrosine phosphatase (PTP). We can also measure the concentration of enzyme using the property of absorbance. Spectrophotometry ... Phosphatases catalyze the hydrolysis of pNPP liberating inorganic phosphate and the conjugate base of para-nitrophenol (pNP). ...
It specifies a protein with structural features similar to members of the non-receptor-type protein-tyrosine phosphatase family ... dual-specificity protein tyrosine phosphatases". Molecules and Cells. 8 (1): 2-11. PMID 9571625. Keyse SM (Apr 1998). "Protein ... Keyse SM, Emslie EA (Oct 1992). "Oxidative stress and heat shock induce a human gene encoding a protein-tyrosine phosphatase". ... "The growth factor-inducible immediate-early gene 3CH134 encodes a protein-tyrosine-phosphatase". Proceedings of the National ...
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. Protein tyrosine phosphatases ... "Receptor protein tyrosine phosphatases, cell adhesion and signal transduction". Advances in Protein Phosphatases. 8: 241-71. ... "Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine ... Rosdahl JA, Mourton TL, Brady-Kalnay SM (2002). "Protein kinase C delta (PKCdelta) is required for protein tyrosine phosphatase ...
Martell KJ, Angelotti T, Ullrich A (1998). "The "VH1-like" dual-specificity protein tyrosine phosphatases". Mol. Cells. 8 (1): ... Dual specificity protein phosphatase 10 is an enzyme that in humans is encoded by the DUSP10 gene. Dual specificity protein ... Tanoue, T; Yamamoto T; Maeda R; Nishida E (Jul 2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 ... Tanoue T, Yamamoto T, Maeda R, Nishida E (2001). "A Novel MAPK phosphatase MKP-7 acts preferentially on JNK/SAPK and p38 alpha ...
Liu F, Hill DE, Chernoff J (1996). "Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src ... a novel mechanism of protein tyrosine phosphatase substrate recognition". Oncogene. 15 (8): 877-85. doi:10.1038/sj.onc.1201279 ... "Fyn and Lck tyrosine kinases regulate tyrosine phosphorylation of p105CasL, a member of the p130Cas docking protein family, in ... novel SH2-containing protein family), and other proteins such as the Id family of helix-loop-helix proteins. In terms of post- ...
Receptor-type tyrosine-protein phosphatase F is an enzyme that in humans is encoded by the PTPRF gene. The protein encoded by ... "Insulin receptor protein-tyrosine phosphatases. Leukocyte common antigen-related phosphatase rapidly deactivates the insulin ... "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions". ... "The LAR transmembrane protein tyrosine phosphatase and a coiled-coil LAR-interacting protein co-localize at focal adhesions". ...
Tiganis T (January 2002). "Protein tyrosine phosphatases: dephosphorylating the epidermal growth factor receptor". IUBMB Life. ... Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function". Molecular and Cellular ... "Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. ... "Phosphotyrosine 1173 mediates binding of the protein-tyrosine phosphatase SHP-1 to the epidermal growth factor receptor and ...
CagA then allosterically activates protein tyrosine phosphatase/protooncogene Shp2. Pathogenic strains of H. pylori have been ... Once inside the cell, the CagA protein is phosphorylated on tyrosine residues by a host cell membrane-associated tyrosine ... The other four families are porins, iron transporters, flagellum-associated proteins, and proteins of unknown function. Like ... independent of protein tyrosine phosphorylation. A great deal of diversity exists between strains of H. pylori, and the strain ...
His research is mainly focused on studying the function and regulation of protein tyrosine phosphatases. He did his ... Tonks, Nicholas K. (2006). "Protein tyrosine phosphatases: from genes, to function, to disease". Nature Reviews Molecular Cell ... After graduation, he joined Sir Philip Cohen lab in University of Dundee for his PhD study in protein phosphatase from 1982- ... "MRC Protein Phosphorylation Unit :: Research :: Philip Cohen :: Profiles for Past Lab Members". Ppu.mrc.ac.uk. Retrieved 5 May ...
A 170 amino acid domain, the so-called MAM (meprin, A-5 protein, and receptor protein-tyrosine phosphatase mu) domain, has been ... a developmentally-regulated cell surface protein; Xenopus nrp1; P28824); and receptor-like tyrosine protein phosphatase. The ... expression and chromosomal localization of a new putative receptor-like protein tyrosine phosphatase". FEBS Lett. 290 (1): 123- ... These proteins have a modular, receptor-like architecture comprising a signal peptide, an N-terminal extracellular domain, a ...
Imai discovered three kinds of protein tyrosine phosphatase (PTP) genes having the function of controlling the signal ... "Mammalian SH2-containing protein tyrosine phosphatase". Cell. 85 (1): 15. doi:10.1016/s0092-8674(00)81077-6. PMID 8620532. ... similarity in genomic organization within protein-tyrosine phosphatasegenes". Oncogene. 9 (10): 3031-3035. PMID 8084610. Adachi ...
PTPLAD2 is a protein tyrosine phosphatase. The exact function of KIAA1797 is not yet understood by the scientific community. It ... KIAA1797 is a protein that in humans is encoded by the KIAA1797 gene. A specific single-nucleotide polymorphism rs7875153 in ... KIAA1797 is a protein-coding gene in Homo sapiens. Alternate names for the gene are FLJ20375, OTTHUMP00000069845, and ... The main isoform of the human protein is 1801 amino acids long, a total of 200,072 Da. Two distinct domains of unknown function ...
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... Protein tyrosine phosphatase non-receptor type 7 is an enzyme that in humans is encoded by the PTPN7 gene. ... "Entrez Gene: PTPN7 protein tyrosine phosphatase, non-receptor type 7". Pettiford SM, Herbst R (February 2000). "The MAP-kinase ... Adachi M, Sekiya M, Arimura Y, Takekawa M, Itoh F, Hinoda Y, Imai K, Yachi A (1992). "Protein-tyrosine phosphatase expression ...
Kwak SP, Dixon JE (Jan 1995). "Multiple dual specificity protein tyrosine phosphatases are expressed and regulated ... The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases ... "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases". Genomics. 22 (2): 462-4. doi:10.1006/geno. ... a dual specificity MAP kinase protein phosphatase". Proteins. 66 (1): 253-8. doi:10.1002/prot.21224. PMID 17078075. S2CID ...
"Association of inhibitory tyrosine protein kinase p50csk with protein tyrosine phosphatase PEP in T cells and other hemopoietic ... Protein tyrosine phosphatase, non-receptor type 22 (lymphoid), also known as PTPN22, is a protein that in humans is encoded by ... The proteins are located in the cytoplasm.[citation needed] This gene encodes a protein tyrosine phosphatase which is expressed ... requirements for association of protein-tyrosine phosphatase PEP with the Src homology 3 domain of inhibitory tyrosine protein ...
Computational chemistry Protein tyrosine phosphatase India portal Biology portal Under the guidance of Tom Blundell, a Knight ... "Modulation of Catalytic Activity in Multi-Domain Protein Tyrosine Phosphatases". PLOS ONE. 6 (9): e24766. Bibcode:2011PLoSO... ... She was the lead developer of 3DSwap, a database of 3D domain-swapped proteins. Besides, along with James Spudich of the ... Sowdhamini's research is in the fields of computational studies of Protein Science as well as genome sequencing and she is ...
"SH2 Domain-Mediated Interaction of Inhibitory Protein Tyrosine Kinase Csk with Protein Tyrosine Phosphatase-HSCF". Mol. Cell. ... The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... 2001). "Cytoskeletal protein PSTPIP1 directs the PEST-type protein tyrosine phosphatase to the c-Abl kinase to mediate Abl ... A Tyrosine Phosphorylated Cleavage Furrow-associated Protein that Is a Substrate for a PEST Tyrosine Phosphatase". J. Cell Biol ...
Cho H (2013). "Protein tyrosine phosphatase 1B (PTP1B) and obesity". Vitamins and Hormones. 91: 405-24. doi:10.1016/B978-0-12- ... similar to squalamine that is an allosteric inhibitor of protein-tyrosine phosphatase 1B (PTP1B). It was isolated from the ...
Protein tyrosine phosphatase, mitochondrial 1 is a Protein, in humans is primarily coded by the gene PTPMT1 gene. ... "Entrez Gene: Protein tyrosine phosphatase, mitochondrial 1". Retrieved 2017-01-12. Niemi NM, Lanning NJ, Westrate LM, MacKeigan ... of all the structure information available in the PDB for Mouse Phosphatidylglycerophosphatase and protein-tyrosine phosphatase ... JP (2013). "Downregulation of the mitochondrial phosphatase PTPMT1 is sufficient to promote cancer cell death". PLOS ONE. 8 (1 ...
... tyrosine phosphatase family and encodes a single-pass type I membrane protein with two cytoplasmic tyrosine-protein phosphatase ... "Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases ... Receptor-type tyrosine-protein phosphatase zeta also known as phosphacan is an enzyme that in humans is encoded by the PTPRZ1 ... "Entrez Gene: PTPRZ1 protein tyrosine phosphatase, receptor-type, Z polypeptide 1". Krueger NX, Saito H (1992). "A human ...
Non-receptor tyrosine-protein kinase TYK2. Protein-tyrosine phosphatases PTPN3 and PTPN4, enzymes that appear to act at ... Protein-tyrosine phosphatases PTPN14 and PTP-D1, PTP-RL10 and PTP2E. Caenorhabditis elegans protein phosphatase ptp-1. Chishti ... Focal-adhesion kinases (FAKs), cytoplasmic protein tyrosine kinases involved in signalling through integrins. Janus tyrosine ... Ezrin, moesin, and radixin are highly related proteins (ERM protein family), but the other proteins in which the FERM domain is ...
"Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases ... The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... Receptor-type tyrosine-protein phosphatase gamma is an enzyme that in humans is encoded by the PTPRG gene. ... Jul 1991). "Receptor protein-tyrosine phosphatase gamma is a candidate tumor suppressor gene at human chromosome region 3p21". ...
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... "Protein tyrosine phosphatase epsilon inhibits signaling by mitogen-activated protein kinases". Mol. Cancer Res. 1 (7): 541-50. ... "Phosphorylation-dependent regulation of Kv2.1 Channel activity at tyrosine 124 by Src and by protein-tyrosine phosphatase ... "Expression of human protein tyrosine phosphatase epsilon in leucocytes: a potential ERK pathway-regulating phosphatase". Scand ...
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... Receptor-type tyrosine-protein phosphatase S, also known as R-PTP-S, R-PTP-sigma, or PTPσ, is an enzyme that in humans is ... a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611-20. doi: ... a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611-20. doi: ...
The protein encoded by this gene is a member of the protein tyrosine phosphatase (PTP) family. PTPs are known to be signaling ... "Multiple interactions between receptor protein-tyrosine phosphatase (RPTP) alpha and membrane-distal protein-tyrosine ... a family of LAR transmembrane protein-tyrosine phosphatase-interacting proteins". J. Biol. Chem. 273 (25): 15611-20. doi: ... "Entrez Gene: PTPRD protein tyrosine phosphatase, receptor type, D". Lei N, et al. (2010). "Autism Is Associated with Inherited ...
1993). "PAC-1: a mitogen-induced nuclear protein tyrosine phosphatase". Science. 259 (5102): 1763-6. doi:10.1126/science. ... The protein encoded by this gene is a member of the dual specificity protein phosphatase subfamily. These phosphatases ... "Chromosomal localization of four human VH1-like protein-tyrosine phosphatases" (PDF). Genomics. 22 (2): 462-4. doi:10.1006/geno ... Dual specificity protein phosphatase 2 is an enzyme that in humans is encoded by the DUSP2 gene. ...
Tyrosine phosphatase. *PTEN *Bannayan-Riley-Ruvalcaba syndrome. *Lhermitte-Duclos disease. *Cowden syndrome ... Mutations in the RPS6KA3 disturb the function of the protein, but it is unclear how a lack of this protein causes the signs and ... The RPS6KA3 gene makes a protein that is involved with signaling within cells. Researchers believe that this protein helps ... The protein RSK2 which is encoded by the RPS6KA3 gene is a kinase which phosphorylates some substrates like CREB and histone H3 ...
The elimination half-life is around 2 hours.[8][118] It is moderately bound to plasma proteins, especially albumin.[8] However ... and with 250 mg/kg mildly elevated Alkaline phosphatase and Gamma-GT. Studies in dogs revealed no toxicity relevant for humans ... Substrates→Products: Phenylalanine→Tyrosine. *Inhibitors: 3,4-Dihydroxystyrene. TH. *Substrates→Products: Tyrosine→L-DOPA ( ... binding to cAMP-dependent protein kinase (PKA).[111] ...
Regulation by the CD45 tyrosine phosphatase.". J. Immunol. 145 (8): 2448-54. PMID 1976695.. ... 1992). "The lymphocyte-specific tyrosine protein kinase p56lck is endocytosed in Jurkat cells stimulated via CD2.". J. Immunol. ... Wilkins A, Yang W, Yang J (2003). "Structural biology of the cell adhesion protein CD2: from molecular recognition to protein ... 1990). "Immunoregulatory effect of a synthetic peptide corresponding to a region of protein p24 of HIV.". Folia Biol. (Praha) ...
Shiota M, Fujimoto J, Semba T, Satoh H, Yamamoto T, Mori S (Jun 1994). "Hyperphosphorylation of a novel 80 kDa protein-tyrosine ... Prostatic acid phosphatase. *Glutamate carboxypeptidase II. *erbB-3 receptor. *Early prostate cancer antigen-2 ... CD30, also known as TNFRSF8, is a cell membrane protein of the tumor necrosis factor receptor family and tumor marker. ... Proteins: clusters of differentiation (see also list of human clusters of differentiation) ...
CD45 - a transmembrane protein whose intracellular tail functions as a tyrosine phosphatase that activates Src family kinases ... UMich Orientation of Proteins in Membranes protein/pdbid-2hac - Zeta-zeta dimer of T cell receptor ... and regulation of molecules beneath the lipid bilayer is via reversible tyrosine phosphorylation by protein kinase/phosphatase ... to bind to the ITAM and activated ZAP-70 phosphorylates tyrosines on the adaptor protein LAT, which then attracts PLC-γ. Other ...
protein binding. • heme binding. • electron carrier activity. Cellular component. • cytosol. • protein phosphatase type 2A ... or nitrogen dioxide NO2 in the mitochondria can be lethal since they nitrate tyrosine residues of cytochrome c which leads to ... protein serine/threonine phosphatase activity. • metal ion binding. • ... Favre B, Zolnierowicz S, Turowski P, Hemmings BA (Jun 1994). "The catalytic subunit of protein phosphatase 2A is carboxyl- ...
phosphatase binding. • phosphoprotein phosphatase activity. • ion channel binding. • cytoskeletal protein binding. • protein C- ... "Human homologue of the Drosophila discs large tumor suppressor binds to p56lck tyrosine kinase and Shaker type Kv1.3 potassium ... protein binding. • protein complex scaffold activity. • protein kinase binding. • L27 domain binding. • ligand-gated ion ... SAP97 is a mammalian MAGUK-family member protein that is similar to the Drosophila protein Dlg1 (the protein is alternatively ...
Tyrosine:. *protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase. *Sh2 domain-containing protein tyrosine ... GTP-binding protein regulators regulate G proteins in several different ways. Small GTPases act as molecular switches in ... and thus requires another class of regulatory proteins to accelerate this activity, the GTPase activating proteins (GAPs). ... GTP-Binding+Protein+Regulators at the US National Library of Medicine Medical Subject Headings (MeSH) ...
Tyrosine phosphatase. *PTEN *Bannayan-Riley-Ruvalcaba syndrome. *Lhermitte-Duclos disease. *Cowden syndrome ... Deficiencies of intracellular signaling peptides and proteins. GTP-binding protein regulators. GTPase-activating protein. * ...
... which contain residues that can be directly modified by a series of protein kinases and protein phosphatases, as well as ... Yu XM, Askalan R, Keil GJ, Salter MW (January 1997). "NMDA channel regulation by channel-associated protein tyrosine kinase Src ... The NMDA receptor is a glutamate and ion channel protein receptor that is activated when glycine and glutamate bind to it.[2] ... The NMDA receptor is ionotropic, meaning it is a protein which allows the passage of ions through the cell membrane.[4] The ...
The phosphorylated tyrosine residue can then serve as a docking site for downstream signaling proteins.[21] (Fig. 1). ... Phosphorylation is easily reversed by phosphatases. Therefore, it is an effective method of turning 'on' and 'off' kinase ... a b c d e f g h i j k l m Petsko, GA and Ringe, D 2009, 'Protein Structure and Function', Oxford University Press Inc., New ... threonine or tyrosine residues within protein kinases, normally to regulate the catalytic activity.[3][4] Autophosphorylation ...
"Tyrosine phosphorylation acts as a molecular switch to full-scale activation of the eIF2alpha RNA-dependent protein kinase". ... "The inhibitor-1 C terminus facilitates hormonal regulation of cellular protein phosphatase-1: functional implications for ... protein phosphorylation. • SREBP signaling pathway. • positive regulation of signal transduction. • ribosome assembly. • ... Squatrito M، Mancino M، Sala L، Draetta GF (Jun 2006). "Ebp1 is a dsRNA-binding protein associated with ribosomes that ...
protein tyrosine kinase activity. • protein phosphatase binding. 細胞の構成要素. • 細胞質. • 細胞質基質. • 膜. • 焦点接着. • extrinsic component of ... "Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts". The Journal ... protein kinase activity. • JUN kinase binding. • non-membrane spanning protein tyrosine kinase activity. • transferase activity ... FAK(focal adhesion kinase、フォーカルアドヒージョンキナーゼ、焦点接着キナーゼ、接着斑
... which in turn activates protein phosphatases PP1 and calcineurin. However, AMPAR endocytosis has also been activated by voltage ... tyrosine produces beneficial effects in experimental stroke and seizures". Amino Acids. 40 (4): 1151-1158. doi:10.1007/s00726- ... Transmembrane AMPA receptor regulatory proteins (TARPs) are a family proteins that associate with AMPA receptors and control ... parts of the protein that pass through the plasma membrane), proteins interacting with the subunit indicated that the N- ...
Peles E, Schlessinger J, Grumet M (1998). «Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: ... 1999). «The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional ... a novel non-proteoglycan variant of phosphacan/receptor protein tyrosine phosphatase-beta, interacts with neuronal receptors ... 1995). «The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell ...
Protein phosphatase: Protein tyrosine phosphatase. *Protein serine/threonine phosphatase. *Dual-specificity phosphatase ... protein binding. • hydrolase activity. • protein kinase binding. • serine hydrolase activity. Cellular component. • cytoplasm. ... protein phosphorylation. • long-chain fatty acid catabolic process. • metabolism. • triglyceride catabolic process. ... Syu LJ, Saltiel AR (1999). "Lipotransin: a novel docking protein for hormone-sensitive lipase". Mol. Cell. 4 (1): 109-15. doi: ...
Activated protein kinase C inhibits the tyrosine kinase activity of epidermal growth factor receptor (EGFR), the rational ... "Regulation of hemolysin expression and virulence of Staphylococcus aureus by a serine/threonine kinase and phosphatase". PLOS ... Protein: cell membrane proteins (other than Cell surface receptor, enzymes, and cytoskeleton) ... "Thermostable direct hemolysin diminishes tyrosine phosphorylation of epidermal growth factor receptor through protein kinase C ...
"Receptor protein tyrosine phosphatase PTPmu associates with cadherins and catenins in vivo". The Journal of Cell Biology. 130 ( ... "Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT)". Brain Research. 1116 (1 ... protein binding. • ankyrin binding. • gamma-catenin binding. • beta-catenin binding. • GTPase activating protein binding. • ... Oneyama C, Nakano H, Sharma SV (March 2002). "UCS15A, a novel small molecule, SH3 domain-mediated protein-protein interaction ...
Hayashi T, Umemori H, Mishina M, Yamamoto T: The AMPA receptor interacts with and signals through the protein tyrosine kinase ... Flajolet M, Rakhilin S, Wang H, et al.: Protein phosphatase 2C binds selectively to and dephosphorylates metabotropic glutamate ... Hirbec H, Perestenko O, Nishimune A, et al.: The PDZ proteins PICK1, GRIP, and syntenin bind multiple glutamate receptor ... Er ist ein menschliches Protein.[1]. Glutamat-Rezeptoren gehören zu den vorherrschenden exzitatorischen Neurotransmitter- ...
Tyrosine:. *protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase. *Sh2 domain-containing protein tyrosine ... protein complex binding. • signal transducer activity. • protein binding. • GTPase activity. • GTPase binding. • G-protein ... protein heterotrimerization. • Wnt signaling pathway, calcium modulating pathway. • protein folding. • G-protein coupled ... Guanine nucleotide-binding protein G(I)/G(S)/G(T) subunit beta-1 is a protein that in humans is encoded by the GNB1 gene.[5] ...
Peles E, Schlessinger J, Grumet M (Apr 1998). "Multi-ligand interactions with receptor-like protein tyrosine phosphatase beta: ... a novel non-proteoglycan variant of phosphacan/receptor protein tyrosine phosphatase-beta, interacts with neuronal receptors ... "The interaction between F3 immunoglobulin domains and protein tyrosine phosphatases zeta/beta triggers bidirectional signalling ... "The carbonic anhydrase domain of receptor tyrosine phosphatase beta is a functional ligand for the axonal cell recognition ...
Protein tyrosine phosphatase receptor type O, also known as glomerular epithelial protein 1 (GLEPP1), has been shown to be ... Additionally, the protein in the urine causes it to become frothy. For years, pathologists found no changes when viewing ... When urine protein levels have normalised, corticosteroids are gradually withdrawn over several weeks (to avoid triggering an ... When the urine is clear of protein, the medications can be discontinued. Fifty percent of patients will relapse and need ...
protein serine/threonine kinase inhibitor activity. • phosphatase binding. • stem cell factor receptor binding. • protein ... Spread-1 is a member of the Sprouty family of proteins and is phosphorylated by tyrosine kinase in response to several growth ... Sprouty-related, EVH1 domain-containing protein 1 (Spread-1) is a protein that in humans is encoded by the SPRED1 gene located ... protein kinase binding. Cellular component. • membrane. • plasma membrane. • caveola. • cytosol. • cell nucleus. • cytoplasmic ...
Zhu X, Sen J, Stevens L, Goltz JS, Stein D (Sep 2005). "Drosophila pipe protein activity in the ovary and the embryonic ... and acid/base phosphatase. Prior to the realization that individual enzymes were capable of such a task, it was believed that ... which can act on tyrosine, phenylalanine, and tryptophan, it reversibly transfers an amino group from one molecule to the other ... "1aqy Summary". Protein Data Bank in Europe Bringing Structure to Biology. The European Bioinformatics Institute. Retrieved 11 ...
Click on genes, proteins and metabolites below to visit Gene Wiki pages and related Wikipedia articles. The pathway can be ... "Regulation of pyruvate dehydrogenase kinase and phosphatase by acetyl-CoA/CoA and NADH/NAD ratios". Biochemical and ... Acetyl-CoA (acetyl coenzyme A) is a molecule that participates in many biochemical reactions in protein, carbohydrate and lipid ... Acetyl-CoA is also the source of the acetyl group incorporated onto certain lysine residues of histone and nonhistone proteins ...
Peripheral membrane protein. *Phenethylamine. *Phenylalanine. *Fosfaigin Phosphagen. *Fosfatáis phosphatase. *Fosfailipid ... Tyrosine. U[cuir in eagar , athraigh foinse]. *Ubiquitin. *Úraicil Uracil. *Úiré Urea ...
"Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha". Cancer Res. 62 (22): 6357-61. PMID ... BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases". Oncogene. 15 (2): 143-57. ... Breast cancer type 1 susceptibility protein is a protein that in humans is encoded by the BRCA1 (/ˌbrækəˈwʌn/) gene.[5] ... protein binding. • transcription coactivator activity. • androgen receptor binding. • RNA binding. • ubiquitin protein ligase ...
Protein phosphatase: Protein tyrosine phosphatase. *Protein serine/threonine phosphatase. *Dual-specificity phosphatase ... Mutations of the glucose 6-phosphatase system, to be specific the glucose 6-phosphatase-α subunit (glucose 6-phosphatase-α), ... Wikimedia Commons has media related to Glucose 6-phosphatase.. *Glucose-6-Phosphatase at the US National Library of Medicine ... Glucose 6-phosphatase is a complex of multiple component proteins, including transporters for G6P, glucose, and phosphate. The ...
Latour S, Veillette A (June 2001). "Proximal protein tyrosine kinases in immunoreceptor signaling". Curr. Opin. Immunol. 13 (3 ... "Autoimmune-associated PTPN22 R620W variation reduces phosphorylation of lymphoid phosphatase on an inhibitory tyrosine residue" ... Nada S, Okada M, MacAuley A, Cooper JA, Nakagawa H (May 1991). "Cloning of a complementary DNA for a protein-tyrosine kinase ... Sun G, Budde RJ (September 1997). "Expression, purification, and initial characterization of human Yes protein tyrosine kinase ...
Pettiford, S M; Herbst R (2000). „The MAP-kinase ERK2 is a specific substrate of the protein tyrosine phosphatase HePTP". ... Protein kinaza C (EC 2.7.11.13). Protein kinaza C, Protein kinaza Cζ, PKC alfa, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, ... Protein kinaza C (EC 2.7.11.13). Protein kinaza C, Protein kinaza Cζ, PKC alfa, PRKCB1, PRKCD, PRKCE, PRKCH, PRKCG, PRKCI, ... 1999). „Inhibition of T cell signaling by mitogen-activated protein kinase-targeted hematopoietic tyrosine phosphatase (HePTP ...
... and laboratory protocols on the more essential aspects of protein tyrosine phosphatase (PTP) function and regulation, including ... Protein Tyrosine Phosphatases. Book Subtitle. Methods and Protocols. Editors. * Rafael Pulido Series Title. Methods in ... Authoritative and practical, Protein Tyrosine Phosphatases: Methods and Protocols aims to aid researchers in better defining ... Tailor-Made Protein Tyrosine Phosphatases: In Vitro Site-Directed Mutagenesis of PTEN and PTPRZ-B ...
Protein tyrosine phosphatases take off.. Barford D1, Jia Z, Tonks NK. ... Protein tyrosine phosphatases (PTPs) are a family of signal transduction enzymes that dephosphorylate phosphotyrosine ... Protein Tyrosine Phosphatases/chemistry*. *Protein Tyrosine Phosphatases/physiology*. *Protein Tyrosine Phosphatases/ ... containing proteins. Structural and kinetic studies provide a molecular understanding of how these enzymes regulate a wide ...
... belong to the superfamily of protein-tyrosine phosphatases and have the intrinsic ability to transduce signals across the cell ... Receptor Protein-Tyrosine Phosphatases (RPTPs) belong to the superfamily of protein-tyrosine phosphatases and have the ... Receptor protein-tyrosine phosphatase signalling in development Int J Dev Biol. 1999;43(7):723-33. ... Protein Tyrosine Phosphatases / metabolism * Protein Tyrosine Phosphatases / physiology* * Receptor-Like Protein Tyrosine ...
Oxidative Modification of Protein Tyrosine Phosphatases Message Subject. (Your Name) has forwarded a page to you from Science ...
Oxidative Modification of Protein Tyrosine Phosphatases Message Subject. (Your Name) has forwarded a page to you from Science ... Because protein tyrosine phosphatases (PTPs) all harbor an absolutely conserved catalytic cysteine residue, oxidation of this ... Therefore, tyrosine phosphorylation-dependent signaling involving receptor tyrosine kinases, mitogen-activated protein kinases ... We describe a nonradioisotopic method that discriminates between reduced and oxidatively modified tyrosine phosphatases, thus ...
Protein tyrosine phosphatase 1B negatively regulates integrin signaling.. Liu F1, Sells MA, Chernoff J. ... Protein tyrosine phosphatase (PTP) 1B has long been known to regulate cell proliferation negatively, but the mechanism by which ... We have shown previously that PTP1B binds to, and dephosphorylates, p130(Cas) (Crk-associated substrate) [1], a protein that is ... In rat fibroblasts that overexpress PTP1B, the activation of mitogen-activated protein (MAP) kinase by growth factors was not ...
The family of protein tyrosine phosphatases (PTPs) play critical roles in celluar signalling pathways and are recognised as ... However, development of therapeutics targeting the family of protein tyrosine phosphatases has lagged far behind that of ...
Therapies that target the TK enzymatic counterparts, the multi-enzyme family of protein tyrosine phosphatases (PTPs), are still ... Over the years, however, many different protein interaction-based regulatory mechanisms that control PTP activity have been ... Attempts to normalize aberrant tyrosine phosphorylation levels in disease states currently involve either the application of ... small compounds that inhibit tyrosine kinases (TKs) or the addition of growth factors or their mimetics to boost receptor-type ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... Protein family membership. *Protein-tyrosine phosphatase, non-receptor type-6, -11 (IPR012152) ... GO:0006470 protein dephosphorylation GO:0016311 dephosphorylation Molecular Function. GO:0004725 protein tyrosine phosphatase ...
We combine protein signatures from a number of member databases into a single searchable resource, capitalising on their ... InterPro provides functional analysis of proteins by classifying them into families and predicting domains and important sites ... GO:0006470 protein dephosphorylation GO:0016311 dephosphorylation Molecular Function. GO:0004725 protein tyrosine phosphatase ...
Regulation of the Protein Tyrosine Phosphatase TCPTP Lead researcher. Professor T Tiganis ...
Protein Tyrosine Phosphatase-1B Gene PTPN1. Nicola J. Spencer-Jones, Xiaoling Wang, Harold Snieder, Tim D. Spector, Nicholas D. ... Protein Tyrosine Phosphatase-1B Gene PTPN1. Nicola J. Spencer-Jones, Xiaoling Wang, Harold Snieder, Tim D. Spector, Nicholas D. ... Protein Tyrosine Phosphatase-1B Gene PTPN1. Selection of Tagging Single Nucleotide Polymorphisms and Association With Body Fat ... Protein tyrosine phosphatase-1B (PTP-1B) negatively regulates the signaling pathways of insulin and leptin, two hormones ...
The protein tyrosine phosphatase (PTP) family is involved in multiple cellular functions and plays an important role in various ... protein-tyrosine phosphatase inhibitors; hepatocellular carcinoma; signaling pathways; therapeutic targets protein-tyrosine ... The protein tyrosine phosphatase (PTP) family is involved in multiple cellular functions and plays an important role in various ... The Roles of Protein Tyrosine Phosphatases in Hepatocellular Carcinoma. Yide Huang 1,2. ...
TYROSINE-PROTEIN PHOSPHATASE NON-RECEPTOR TYPE 1. A. 304. Homo sapiens. Mutation(s): 0 Gene Names: PTPN1 (PTP1B). EC: 3.1.3.48 ... Crystal structures of protein-tyrosine phosphatase 1B in complex with compounds bearing a novel isothiazolidinone (IZD) ... Crystal structures of protein-tyrosine phosphatase 1B in complex with compounds bearing a novel isothiazolidinone (IZD) ... Structural Basis for Inhibition of Protein-Tyrosine Phosphatase 1B by Isothiazolidinone Heterocyclic Phosphonate Mimetics.. Ala ...
... is a phospho tyrosine-specific protein phosphatase. It is a truncated form of the human T-Cell protein tyrosine phosphatase ( ... 1X NEBuffer for Protein Tyrosine Phosphatases (PTP) Incubate at 30°C 1X NEBuffer for Protein Tyrosine Phosphatases (PTP) 50 mM ... T-Cell Protein Tyrosine Phosphatase (TC PTP) is a phospho tyrosine-specific protein phosphatase. It is a truncated form of the ... The Protein Tyrosine Phosphatase (PTP) activity of TC PTP is assessed on MyBP phosphorylated exclusively on tyrosine residues ...
A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1. Richard L. Haspel and James E. Darnell Jr. ... A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1 ... A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1 ... A nuclear protein tyrosine phosphatase is required for the inactivation of Stat1 ...
We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic ... Here, we have described a mechanism of NLRP3 inflammasome regulation by tyrosine phosphorylation of NLRP3 at Tyr861. ... Together, our results identify tyrosine phosphorylation as an important regulatory mechanism for NLRP3 that prevents aberrant ... NLRP3 tyrosine phosphorylation is controlled by protein tyrosine phosphatase PTPN22. Marianne R. Spalinger, … , Gerhard Rogler ...
PROTEIN-TYROSINE PHOSPHATASE. A. 321. Homo sapiens. Mutation(s): 0 Gene Names: PTPN1, PTP1B. EC: 3.1.3.48. ... Protein tyrosine phosphatase 1B with active site inhibitor. *DOI: 10.2210/pdb1WAX/pdb ... The method is illustrated against five proteins (p38 MAP kinase, CDK2, thrombin, ribonuclease A, and PTP1B). The fragments ... The method is illustrated against five proteins (p38 MAP kinase, CDK2, thrombin, ribonuclease A, and PTP1B) ... ...
View protein in PROSITE. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 2 hits. PS50055. TYR_PHOSPHATASE_PTP. 2 ... View protein in PROSITE. PS00383. TYR_PHOSPHATASE_1. 1 hit. PS50056. TYR_PHOSPHATASE_2. 2 hits. PS50055. TYR_PHOSPHATASE_PTP. 2 ... Protein tyrosine phosphate + H2O = protein tyrosine + phosphate.UniRule annotation. ,p>Information which has been generated by ... View protein in InterPro. IPR029021. Prot-tyrosine_phosphatase-like. IPR000242. PTPase_domain. IPR016130. Tyr_Pase_AS. ...
... and protein tyrosine phosphate + H2O = protein tyrosine + phosphate.. Synonyms. dual-specificity protein phosphatase View GO ... Catalysis of the reactions: protein serine + H2O = protein serine + phosphate; protein threonine phosphate + H2O = protein ... Gene Ontology Term: protein tyrosine/serine/threonine phosphatase activity. GO ID. GO:0008138 Aspect. Molecular Function. ...
3 Abstracts with Protein tyrosine phosphatase 1B (PTP1B) modulator Research. Filter by Study Type. Animal Study. ... 1 Substances Researched for Protein tyrosine phosphatase 1B (PTP1B) modulator Name. AC. CK. Focus. ... Pharmacological Actions : Hypoglycemic Agents, Insulin Sensitizers, Protein tyrosine phosphatase 1B (PTP1B) modulator ...
1995) Protein-tyrosine-phosphatase SHPTP2 is a required positive effector for insulin downstream signaling. Proc Natl Acad Sci ... The protein tyrosine phosphatase Shp2 is a positive regulator of growth factor signaling. Gain-of-function mutations in several ... The protein tyrosine phosphatase (PTP) Shp2 (PTPN11) is mutated in human disease. Activating mutations cause Noonan syndrome (1 ... 2001) Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat Genet 29:465-468. ...
Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal ... An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. ... Protein Tyrosine Phosphatase; Tyrosine Phosphatases, Protein; Phosphotyrosine Phosphatase; Protein-Tyrosine-Phosphatase; ... Protein-Tyrosine Phosphatase; Phosphatase, Phosphotyrosine; Phosphatase, Phosphotyrosyl Protein; Phosphatase, Protein-Tyrosine ...
... Yukio Ikeda,1 Ehud Ziv,2 Eleazar ... Protein tyrosine phosphatases (PTPases) have been suggested to modulate the insulin receptor signal transduction pathways.We ... No changes in the protein expression level of src homology PTPase 2 (SHP-2) (muscle, liver) or leukocyte antigen receptor (LAR ... However, PTP 1B- specific activity (activity/protein) significantly decreased (50% to 56%) in skeletal muscle of diabetic ...
Protein Tyrosine Kinase and Phosphatase Expression Profiling in Cancer Research. Tyrosine kinases (PTK) represent only 10% of ... Protein tyrosine phosphatases (PTP) attenuate growth signals generated by the PTKs through catalyzing the tyrosine ... Protein Tyrosine Kinase and Phosphatase Expression Profiling in Human Cancers. Wen-Chang Lin. Institute of Biomedical Sciences ... 1998) Protein-tyrosine kinase and protein-serine/threonine kinase expression in human gastric cancer cell lines. J. Biomed. Sci ...
... which delete phosphate groups from phosphorylated tyrosine residues on proteins. Protein tyrosine phosphorylation is a known ... post-translational modification that forms detection for protein interactions and cellular localization ...
The Gene Ontology (GO) project is a collaborative effort to address the need for consistent descriptions of gene products across databases. You can use this browser to view terms, definitions, and term relationships in a hierarchical display. Links to summary annotated gene data at MGI are provided in Term Detail reports.
Protein Tyrosine Phosphatases [D08.811.277.352.650.775]. *SH2 Domain-Containing Protein Tyrosine Phosphatases [D08.811.277.352. ... SH2 Domain-Containing Protein Tyrosine Phosphatases*SH2 Domain-Containing Protein Tyrosine Phosphatases ... A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class ... Intracellular Signaling Peptides and Proteins [D12.644.360]. *SH2 Domain-Containing Protein Tyrosine Phosphatases [D12.644. ...
J:212986 Erkens M, et al., Protein tyrosine phosphatase receptor type R deficient mice exhibit increased exploration in a new ... IPR008356 Protein-tyrosine phosphatase, KIM-containing. IPR029021 Protein-tyrosine phosphatase-like. IPR016334 Protein-tyrosine ... protein coding gene. Chr10:116018200-116274932 (.). 129S1/SvImJ MGP_129S1SvImJ_G0017742. protein coding gene. Chr10:118766908- ... protein coding gene. Chr10:114208423-114462338 (+). AKR/J MGP_AKRJ_G0017680. protein coding gene. Chr10:117501343-117760840 (+) ...
Protein-tyrosine-phosphatase that dephosphorylates and probably inhibits MPK6 in non-oxidative stress conditions. In ... Protein-tyrosine-phosphatase PTP1Add BLAST. 340. Proteomic databases. PaxDb, a database of protein abundance averages across ... "Redox control of protein tyrosine phosphatases and mitogen-activated protein kinases in plants.". Gupta R., Luan S.. Plant ... "Redox control of protein tyrosine phosphatases and mitogen-activated protein kinases in plants.". Gupta R., Luan S.. Plant ...
  • We have shown previously that PTP1B binds to, and dephosphorylates, p130(Cas) (Crk-associated substrate) [1], a protein that is thought to play a role in integrin signaling [2,3]. (nih.gov)
  • In rat fibroblasts that overexpress PTP1B, the activation of mitogen-activated protein (MAP) kinase by growth factors was not affected, but activation by cell adhesion was markedly impaired. (nih.gov)
  • We have identified the phenylhydrazonopyrazolone sulfonate PHPS1 as a potent and cell-permeable inhibitor, which is specific for Shp2 over the closely related tyrosine phosphatases Shp1 and PTP1B. (pnas.org)
  • The PTPN1 gene codes for protein tyrosine phosphatase 1B (PTP1B) (EC 3.1.3.48), which negatively regulates insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor kinase activation segment. (diabetesjournals.org)
  • Within one of these type 2 diabetes-associated regions is a positional candidate gene, PTPN1, that codes for the protein tyrosine phosphatase 1B (PTP1B) protein. (diabetesjournals.org)
  • PTP1B is a ubiquitously expressed phosphatase that dephosphorylates phosphotyrosine residues of the active insulin receptor, disrupting the insulin signaling pathway ( 13 , 14 ). (diabetesjournals.org)
  • Here we report the crystal structures of the regulatory sulphenic and irreversible sulphinic and sulphonic acids of protein tyrosine phosphatase 1B (PTP1B), an important enzyme in the negative regulation of the insulin receptor and a therapeutic target in type II diabetes and obesity. (nih.gov)
  • In addition, it may facilitate reactivation of PTP1B by biological thiols and signal a unique state of the protein. (nih.gov)
  • The key role of protein tyrosine phosphatase 1B (PTP1B) in inflammatory responses has focused this study in understanding its implication in liver fibrosis. (bioportfolio.com)
  • Protein tyrosine phosphatase 1B (PTP1B) resided in the ER membrane is known to regulate ER stress. (bioportfolio.com)
  • Most of them gave potent protein phosphatase 1B (PTP1B) inhibitory activitie. (bioportfolio.com)
  • Protein tyrosine phosphatase interacting protein 51 (PTPIP51) interacts both in vitro and in vivo with PTP1B, a protein tyrosine phosphatase involved in cellular regulation. (springer.com)
  • Brobeil A, Graf M, Oeschger S, Steger K, Wimmer M (2010) PTPIP51-a myeloid lineage specific protein interacts with PTP1B in neutrophil granulocytes. (springer.com)
  • Protein tyrosine phosphatase 1B (PTP1B) counteracts leptin signaling and is a therapeutic target for obesity and diabetes. (jneurosci.org)
  • Protein tyrosine-phosphatase 1B (PTP1B) is a negative regulator of insulin signaling. (ahajournals.org)
  • In contrast, increase in PTP1B protein expression occurred only after 24h. (ahajournals.org)
  • TUDCA lowered protein levels of PTP1B and Bip, whereas PTP1B siRNA failed to alter tunicamycin induction of ER stress markers Bip and CHOP. (ahajournals.org)
  • Protein tyrosine phosphatase 1B (PTP1B) is a key enzyme in the counterregulation of insulin signaling, and its physiological modulation depends on H2O2 and glutathione (GSH). (unboundmedicine.com)
  • The detailed study of PTP1B regulation using an enzymatic assay and Western Blot analysis with an antibody against protein glutathionylation revealed that PTP1B was significantly up-regulated by both a maximization of GPx1 activity and by increasing dietary Se supply, reducing its inhibition via glutathionylation. (unboundmedicine.com)
  • Conclusions- PTP1B suppresses cell proliferation and motility in cultured smooth muscle cells treated with PDGF-BB or FGF2, and the phosphatase plays a counter-regulatory role in vascular injury-induced cell proliferation and neointima formation. (ahajournals.org)
  • PTP1B is a ubiquitously expressed nonreceptor phosphatase targeted to several intracellular domains, including the endoplasmic reticulum and focal adhesions. (ahajournals.org)
  • 17 In a separate recent study, we reported that PDGF and FGF but not IGF-1 significantly increased the levels of PTP1B protein in cultured rat aortic smooth muscle cells. (ahajournals.org)
  • Multi-site phosphorylation of the protein tyrosine phosphatase, PTP1B: identification of cell cycle regulated and phorbol ester stimulated sites of phosphorylation. (pubmedcentralcanada.ca)
  • Further evaluation of their biological properties against PTPs revealed that compound 1 inhibited T-cell PTP activity similarly to PTP1B and exhibited moderate selectivity against PTP1B over vaccinia H-1-related phosphatase. (springer.com)
  • Jiang CS, Liang LF, Guo YW (2012) Natural products possessing protein tyrosine phosphatase 1B (PTP1B) inhibitory activity found in the last decades. (springer.com)
  • Tiganis T (2013) PTP1B and TCPTP-nonredundant phosphatases in insulin signaling and glucose homeostasis. (springer.com)
  • Liver-specific PTP1B deletion also protects against high-fat diet-induced endoplasmic reticulum stress response in vivo, as evidenced by decreased phosphorylation of p38MAPK, JNK, PERK, and eIF2α and lower expression of the transcription factors C/EBP homologous protein and spliced X box-binding protein 1. (pubmedcentralcanada.ca)
  • Therefore, tyrosine phosphorylation-dependent signaling involving receptor tyrosine kinases, mitogen-activated protein kinases, Abl, Src, and Pyk2 is known to be initiated or amplified by reactive oxidants. (sciencemag.org)
  • However, development of therapeutics targeting the family of protein tyrosine phosphatases has lagged far behind that of kinases. (soci.org)
  • Attempts to normalize aberrant tyrosine phosphorylation levels in disease states currently involve either the application of small compounds that inhibit tyrosine kinases (TKs) or the addition of growth factors or their mimetics to boost receptor-type TK activity. (mdpi.com)
  • Shp2 acts downstream of many receptor tyrosine kinases such as Met, fibroblast growth factor (FGF), epidermal growth factor (EGF), and insulin receptors ( 10 ). (pnas.org)
  • Tyrosine kinases (PTK) represent only 10% of all protein kinases, although they are the most important protein kinases. (sigmaaldrich.com)
  • PTPRG has been considered a potential tumor suppressor gene based on its function, antagonizing activity of protein tyrosine kinases that often function as oncoproteins. (atlasgeneticsoncology.org)
  • These homologies suggest that PTEN may suppress tumor cell growth by antagonizing protein tyrosine kinases and may regulate tumor cell invasion and metastasis through interactions at focal adhesions. (sciencemag.org)
  • We also developed new computational models to quantitatively predict how receptor dephosphorylation kinetics as rapid as we found for EGFR might differentially control signaling initiated by receptor tyrosine kinases that dimerize in structurally distinct ways observed naturally among the family of receptor tyrosine kinases (RTKs). (upenn.edu)
  • Ultimately, the new quantitative understanding of EGFR regulation by PTPs developed in this thesis significantly refines our understanding of the dynamics of EGFR-mediated signaling, provides a number of additional testable predictions related to fundamental aspects of EGFR signaling complex nucleation and efficacy of EGFR-targeted therapeutics, and offers a basic quantitative framework for exploring the regulation of other receptor tyrosine kinases by PTPs. (upenn.edu)
  • The balance between these processes is under tight control by protein tyrosine kinases (PTKs) and protein tyrosine phosphatases (PTPs). (eur.nl)
  • PTPs are a key group of signal transduction enzymes which, together with protein tyrosine kinases, control the levels of cellular protein tyrosine phosphorylation. (asm.org)
  • Protein tyrosine kinases phosphorylate cellular substrates on tyrosine residues, and much progress has been made over the last 20 years in elucidating their significance in signal transduction (for reviews, see references 26 , 30 , 31 , 33 , 71 , and 72 ). (asm.org)
  • B cell activation and subsequent antibody secretion involve tyrosine phosphorylation, which is tightly regulated by protein tyrosine kinases (PTKs) and receptor-like protein tyrosine phosphatases (RPTPs). (jimmunol.org)
  • Cross-linking B cell antigen receptor (BCR) elicits early signal transduction events, including activation of protein tyrosine kinases, phosphorylation of receptor components, activation of phospholipase C-gamma (PLC-gamma), and increases in intracellular free Ca2+. (rupress.org)
  • Dephosphorylates cellular tyrosine kinases, including PTK2B/PYK2, and thereby regulates signaling via PTK2B/PYK2. (hmdb.ca)
  • Protein tyrosine phosphatases (PTPs) are thought to play an important role as counter-regulatory agents that attenuate or terminate signaling induced by activation of receptor tyrosine kinases. (ahajournals.org)
  • Batzer A, Kirsch S, Hofer HW (1990) Characterization pf two tyrosine-specific protein kinases from pig spleen. (springer.com)
  • Protein tyrosine kinases and phosphatases play a vital role in the regulation of cell growth and differentiation in animal systems. (plantcell.org)
  • Protein kinases are classified into two major groups: serine/threonine kinases and tyrosine kinases, which phosphorylate serine/threonine and tyrosine, respectively. (plantcell.org)
  • We propose that Ang II induces phosphorylation of growth signaling kinases by redox-sensitive regulation of protein tyrosine phosphatases (PTP) in VSMCs and that augmented Ang II signaling in spontaneously hypertensive rats (SHRs) involves oxidation/inactivation and blunted phosphorylation of the PTP, SHP-2. (ahajournals.org)
  • 1-3 In hypertension, increased ROS production leads to vascular smooth muscle cell (VSMC) growth and inflammation through increased activation of c-Src, mitogen-activated protein (MAP) kinases, and PI3K/AKT. (ahajournals.org)
  • Protein tyrosine phosphatases play a critical role in the reversible phosphorylation of proteins, where they remove phosphates from downstream substrates thereby counterbalancing effects of protein tyrosine kinases (PTK). (ahajournals.org)
  • Ang II, through ROS, induces activation of RTKs such as EGFR and PDGFR-β as well as nonreceptor tyrosine kinases, such as c-Src, which interact with numerous PTPs, including SHP-2, to regulate cell function. (ahajournals.org)
  • Chapters covering state-of-the-art technical approaches suitable to decipher the physiologic roles of PTPs, and their involvement in tissue-specific functions, are also included, which will be of utility for both newcomers and experienced researchers in the field of tyrosine- and phosphoinositide- phosphorylation/dephosphorylation. (springer.com)
  • The following information can be used as suggested initial conditions for dephosphorylation of proteins with TC PTP. (neb.com)
  • N-terminal mutants of Stat1, previously shown to remain phosphorylated for a longer time than wild-type Stat1, were able to enter the nucleus and were not inactivated in the presence of staurosporine, directly demonstrating that these mutations affect phosphatase access and/or activity during the normal dephosphorylation of Stat1. (pnas.org)
  • Together with PROTEIN-TYROSINE KINASE, it regulates tyrosine phosphorylation and dephosphorylation in cellular signal transduction and may play a role in cell growth control and carcinogenesis. (curehunter.com)
  • Protein tyrosine phosphatases (PTP) attenuate growth signals generated by the PTKs through catalyzing the tyrosine dephosphorylation step on their substrate proteins. (sigmaaldrich.com)
  • Involved in regulating signaling through ligand-controlled protein tyrosine dephosphorylation. (atlasgeneticsoncology.org)
  • Two compounds, (naphth-2-yl) difluoromethylphosphonic acid (12) and (napthy-1-yl) difluoromethylphosphonic acid (13) have been found to inhibit dephosphorylation of [32P]insulin receptors by PTP-1B, a protein tyrosine phosphatase (PTPase), with IC50 values of 40-50 microM. (biochemj.org)
  • Compound 12 also inhibited PTP-1B-catalysed dephosphorylation of a synthetic tyrosine phosphorylated substrate poly(Glu80-Tyr20) at the same potency, indicating that 12 acted via interaction with the PTPase. (biochemj.org)
  • Several cancer associated cellular pathways have been identified, in which protein phosphorylation and dephosphorylation, especially on tyrosine residues, are one of most abundant regulatory mechanisms. (eur.nl)
  • Whereas noncatalytic domains may target the PTPs to specific intracellular compartments in which the effective local concentration of substrate is high ( 3 , 19 , 51 ), the PTP catalytic domains themselves confer site-selective protein dephosphorylation by recognizing both the phosphotyrosine residue to be dephosphorylated and its flanking amino acids in the substrate. (asm.org)
  • All characterized PTP-like phytases share an active site sequence motif (His-Cys-(X)5-Arg), a two-step, acid-base mechanism of dephosphorylation, and activity towards phosphrylated tyrosine residues, characteristics that are common to all PTP superfamily enzymes. (wikipedia.org)
  • Protein tyrosine phosphatases (PTPs) are a family of signal transduction enzymes that dephosphorylate phosphotyrosine containing proteins. (nih.gov)
  • Because protein tyrosine phosphatases (PTPs) all harbor an absolutely conserved catalytic cysteine residue, oxidation of this residue inactivates PTPs, rendering tyrosine kinase signaling pathways highly sensitive to the local redox environment. (sciencemag.org)
  • The family of protein tyrosine phosphatases (PTPs) play critical roles in celluar signalling pathways and are recognised as potential drug targets in diabetes, cancer and cardiovascular disease. (soci.org)
  • Therapies that target the TK enzymatic counterparts, the multi-enzyme family of protein tyrosine phosphatases (PTPs), are still lacking despite their undisputed involvement in human diseases. (mdpi.com)
  • Over the years, however, many different protein interaction-based regulatory mechanisms that control PTP activity have been uncovered, providing alternative possibilities to control PTPs individually. (mdpi.com)
  • Protein tyrosine phosphatases (PTPs) consist of a large family of enzymes known to play important roles in controlling virtually all aspects of cellular processes. (aacrjournals.org)
  • While the processes that lead to EGFR activation and phosphorylation have been studied in detail, quantitative aspects of the spatiotemporal regulation of EGFR by protein tyrosines phosphatases (PTPs) are not well understood. (upenn.edu)
  • This same separation of time scales does, however, allow PTPs to control EGFR association with adapter proteins that regulate downstream signaling. (upenn.edu)
  • In particular, when important proteins or novel therapeutic targets are identified-like the family of protein tyrosine phosphatases (PTPs) (reviewed in reference 53 )-a structure-function classification of such protein families becomes an invaluable framework for further advances in biomedical science. (asm.org)
  • The classical PTPs, which are the focus of the present study, encompass both transmembrane receptor-like and nontransmembrane enzymes, and the wide spectrum of protein domains present within this family highlight their diverse cellular functions. (asm.org)
  • In addition to posttranslational modification by oxidation, PTPs are regulated by tyrosine (or serine) phosphorylation, 12 which renders the protein active. (ahajournals.org)
  • citation needed] Only a few of the known phytases belong to a superfamily of enzymes called protein tyrosine phosphatases (PTPs). (wikipedia.org)
  • Perhaps the most consequential of such targets within proteins is the reduced sulfhydryl of cysteine residues. (sciencemag.org)
  • It is a truncated form of the human T-Cell protein tyrosine phosphatase (residues 1-317) which lacks a C-terminal regulatory domain (1,2). (neb.com)
  • Protein phosphatase exclusively specific to phospho-tyrosine residues in proteins. (neb.com)
  • TC PTP can be used to release phosphate groups specifically from phospho-tyrosine residues in proteins. (neb.com)
  • An enzyme group that specifically dephosphorylates phosphotyrosyl residues in selected proteins. (curehunter.com)
  • PTPRG shares a PTP domain, involved in dephosphorylating phosphorylated tyrosine residues, with the other receptor-like protein tyrosine phosphatases. (atlasgeneticsoncology.org)
  • Despite these distinct evolutionary origins, we show here that both HLA-Cw3-specific human p58.183 receptors and H-2D d/k-specific mouse Ly49A receptors recruit the same protein tyrosine phosphatases, PTP1C and PTP1D, upon phosphorylation of critical intracytoplasmic tyrosine residues. (jimmunol.org)
  • Activation of the IRs leads to transphosphorylation of tyrosine residues in the IR activation loop, which in turn leads to the enhanced ability of the IRs to phosphorylate target proteins, such as insulin receptor substrates (IRSs). (pubmedcentralcanada.ca)
  • Proper control of the phosphotyrosine content in signal transduction proteins is essential for normal cell behavior and is lost in many pathologies. (mdpi.com)
  • Protein tyrosine phosphatases (PTPases) have been suggested to modulate the insulin receptor signal transduction pathways.We studied PTPases in Psammomys obesus , an animal model of nutritionally induced insulin resistance. (hindawi.com)
  • Protein tyrosine phosphatases regulate signal transduction pathways involving tyrosine phosphorylation and have been implicated in the development of cancer, diabetes, rheumatoid arthritis and hypertension. (nih.gov)
  • These PP-2A inhibitors could be useful tools for studying serine/threonine-phosphatase-mediated signal transduction. (biochemj.org)
  • The reversion of tyrosine phosphorylation is potentially involved in the regulation of the cell cycle and signal transduction (cf. to the contributions by E. Fischer and G. Draetta, this volume). (springer.com)
  • Protein-tyrosine phosphatases (PTPases) are considered to play an important role in signal transduction. (nii.ac.jp)
  • No changes in the protein expression level of src homology PTPase 2 (SHP-2) (muscle, liver) or leukocyte antigen receptor (LAR) (liver) were detected. (hindawi.com)
  • In all, 15 aryl-containing phosphonates have been synthesized and tested for their effect on protein-tyrosine phosphatase (PTPase) activity. (biochemj.org)
  • Orthovanadate (OVA), a protein tyrosine phosphatase (PTPase) inhibitor, exerts contractile effects on smooth muscle in a Rho-kinase-dependent manner, but the precise mechanisms are not elucidated. (ahajournals.org)
  • In this study, we isolated a cDNA encoding a putative protein tyrosine phosphatase (PTPase) from Arabidopsis (referred to as AtPTP1 ). (plantcell.org)
  • The effects of protein tyrosine phosphatase (PTPase) inhibitor phenylarsine oxide (PAO), sodium vanadate (NaVO3) and Zn2+ on salicylic acid (SA) regulated Vicia faba stomatal movement were studied. (cnki.com.cn)
  • Crystal structures of protein-tyrosine phosphatase 1B in complex with compounds bearing a novel isothiazolidinone (IZD) heterocyclic phosphonate mimetic reveal that the heterocycle is highly complementary to the catalytic pocket of the protein. (rcsb.org)
  • When substituted with a phenol, the small inhibitor induces the closed conformation of the protein and displaces all waters in the catalytic pocket. (rcsb.org)
  • Increasing evidence suggests that the cellular redox state is involved in regulating tyrosine phosphatase activity through the reversible oxidization of the catalytic cysteine to sulphenic acid (Cys-SOH). (nih.gov)
  • The protein contains an extracellular carbonic anhydrase-like and fibronectin type III-like domain, a single transmembrane domain, and a cytoplasmic region with 2 tandem catalytic tyrosine phosphatase domains. (atlasgeneticsoncology.org)
  • In addition to their intercellular catalytic domains which bear the phosphatase activity, the RPTPs are cell-surface-receptor-type molecules and in many cases have large extracellular regions. (portlandpress.com)
  • Recombinant Human Protein Tyrosine Phosphatase, non-receptor type 1 (aa 1-321) The protein coding region of the catalytic domain of PTP-1B (amino acids 1-321) was cloned into an E. coli expression vector. (cellsciences.com)
  • The catalytic domain of PTP-1B was overexpressed in E. coli as a soluble protein, and it was purified by conventional column chromatographic techniques. (cellsciences.com)
  • 1988) and the catalytic domains of membrane proteins like CD45 (Tonks et al. (springer.com)
  • Purification and crystallization of the catalytic domain of human protein tyrosine phosphatase 1B expressed in Escherichia coli. (pubmedcentralcanada.ca)
  • Substrate specificities of catalytic fragments of protein tyrosine phosphatases (HPTP beta, LAR, and CD45) toward phosphotyrosylpeptide substrates and thiophosphotyrosylated peptides as inhibitors. (pubmedcentralcanada.ca)
  • Site-directed mutagenesis defined two highly conserved amino acids, cysteine-265 and aspartate-234, as being essential for the phosphatase activity of the AtPTP1 protein, suggesting a common catalytic mechanism for PTPases from all eukaryotic systems. (plantcell.org)
  • TrxR is homodimeric protein in which each monomer includes an FAD prosthetic group, a NADPH binding site and a redox catalytic site. (biovendor.com)
  • Shp2 is a nonreceptor PTP that harbors a classical tyrosine phosphatase domain and two N-terminal Src homology 2 (SH2) domains ( 7 , 8 ). (pnas.org)
  • A subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. (harvard.edu)
  • Cutting edge: Dependence of TCR antagonism on Src homology 2 domain‐containing protein tyrosine phosphatase activity. (currentprotocols.com)
  • The intracellular domain of PTPμ contains a juxtamembrane sequence with homology to cadherins and two phosphatase domains of which only the membrane proximal is catalytically active ( 17 , 18 ). (aacrjournals.org)
  • The predicted PTEN product has a protein tyrosine phosphatase domain and extensive homology to tensin, a protein that interacts with actin filaments at focal adhesions. (sciencemag.org)
  • We determined whether src-homology domain-2-containing protein tyrosine phosphatase 2 (SHP2), a downstream effecter of insulin signaling, is involved in insulin-induced endothelial inflammation. (ahajournals.org)
  • This molecular view of diseases has contributed to the importance of combining primary sequence data with three-dimensional structure and has increased the awareness of computational homology modeling and its potential to elucidate protein function. (asm.org)
  • SRC homology 2 domain-containing phosphatase 2 (SHP2) is a ubiquitously expressed cytosolic protein tyrosine phosphatase. (upenn.edu)
  • N-cadherin is an in vivo substrate for protein tyrosine phosphatase sigma (PTPsigma) and participates in PTPsigma-mediated inhibition of axon growth. (wikigenes.org)
  • A cDNA coding for PTPN13 was isolated during the screening for the substrate of protein kinase A expressed in mammalian oocytes. (biologists.org)
  • PTPN13 is expressed in both mouse and Xenopus oocytes and is a substrate for protein kinase A in vitro and in vivo. (biologists.org)
  • Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. (pubmedcentralcanada.ca)
  • The protein tyrosine phosphatase Shp2 is a positive regulator of growth factor signaling. (pnas.org)
  • The protein tyrosine phosphatase (PTP) Shp2 (PTPN11) is mutated in human disease. (pnas.org)
  • The presence of activated or up-regulated Shp2 protein ( 5 ) in human cancers and other disease makes Shp2 an excellent target for generating interfering substances ( 6 ). (pnas.org)
  • Several direct targets of Shp2 have been identified, including the platelet-derived growth factor receptors [PDGFR ( 13 )/Torso ( 14 )], the multiadaptor protein Gab1 ( 15 ), Csk-binding protein [Cbp/PAG ( 16 )], and paxillin ( 17 ). (pnas.org)
  • Protein tyrosine phosphatase (PTP) Shp2 is a non-receptor PTP that involved in cell signaling and regulation of cell proliferation, differentiation, and migration. (ideaconnection.com)
  • NSC-117199 was identified as a porent inhibitor of the protein tyrosine phosphatase (PTPa) Shp2. (ideaconnection.com)
  • Also disclosed are methods of inhibiting a protein tyrosine phosphatase in a cell and treating cancer through selective inhibition of Shp2. (ideaconnection.com)
  • Downstream of epidermal growth factor receptor (EGFR) and other receptors, SHP2 is activated by binding to phosphotyrosine-containing receptors and adapter proteins, is required for complete extracellular regulated kinase 1/2 (ERK) pathway activity, which promotes cellular proliferation and survival, and regulates other signaling processes. (upenn.edu)
  • We next developed computational models and associated quantitative experimental data sets to gain quantitative understanding of the regulation of protein complexes containing SHP2 and GRB2-associated binder 1 (GAB1), the primary phosphorylated adapter with which SHP2 associates following EGFR activation. (upenn.edu)
  • Striatal-enriched protein tyrosine phosphatase (STEP) is a brain-specific phosphatase that modulates key signaling molecules involved in synaptic plasticity and neuronal function. (aspetjournals.org)
  • Protein tyrosine phosphatase-1B negatively regulates leptin and insulin signaling, potentially contributing to hormonal resistance. (diabetesjournals.org)
  • Protein tyrosine phosphatase-1B (PTP-1B) negatively regulates the signaling pathways of insulin and leptin, two hormones involved in the central regulation of energy balance ( 1 ). (diabetesjournals.org)
  • an N-terminal motif specific for the INSULIN RECEPTOR, and a C-terminal motif specific for the SH3 domain containing proteins. (curehunter.com)
  • Sustained obesity overwhelms the capacity of endoplasmic reticulum (ER) for the folding of proteins leading to insulin resistance. (ahajournals.org)
  • 1 In recent years, many T1D associations have been reported, but only three (major histocompatibility complex, insulin, and cytotoxic T lymphocyte associated protein 4) have been confirmed in several independent studies. (bmj.com)
  • Zhang ZY, Dodd GT, Tiganis T (2015) Protein tyrosine phosphatases in hypothalamic insulin and leptin signaling. (springer.com)
  • Deletion of Protein Tyrosine Phosphatase Nonreceptor Type 2 in Intestinal Epithelial Cells Results in Upregulation of the Related Phosphatase Protein Tyrosine Phosphatase Nonreceptor Type 23. (bioportfolio.com)
  • Knockdown of protein tyrosine phosphatase nonreceptor type 2 () exaggerates IFN-γ-induced intestinal barrier defects, but mice constitutively lacking in epithelial cells (PTPN2xVilCre mice) do not s. (bioportfolio.com)
  • Protein tyrosine phosphatase nonreceptor type 13 (PTPN13) is a tyrosine phosphatase with multiple interacting domains that has been implicated previously in the regulation of apoptosis. (biologists.org)
  • We describe a nonradioisotopic method that discriminates between reduced and oxidatively modified tyrosine phosphatases, thus facilitating studies that may mechanistically link oxidant activity with specific signaling pathways. (sciencemag.org)
  • These proteins bind to the JAKs or receptors and inhibit further activity ( 9 - 12 ). (pnas.org)
  • However, PTP 1B- specific activity (activity/protein) significantly decreased (50% to 56%) in skeletal muscle of diabetic animals, compared with both the diabetes-resistant line and diabetes-prone animals. (hindawi.com)
  • Receptor Signalling Protein Tyrosine Phosphatase Activity. (atlasgeneticsoncology.org)
  • As a transmembrane adhesion receptor, PTPμ has the ability to sense an extracellular signal via its extracellular segment and transduce this signal intracellularly via its phosphatase activity ( 12 - 14 ). (aacrjournals.org)
  • Nine out of the 15 compounds potently inhibited serine/threonine phosphatase PP-2A activity without any effect on serine/threonine phosphatase PP-1 when tested at a concentration as high as 675 microM. (biochemj.org)
  • Affinity-purified STEP fusion protein exhibited phosphatase activity while a mutated form of the STEP fusion protein (Cys300Ser) showed no demonstrable phosphatase activity. (jneurosci.org)
  • Deregulation of PTP activity results in aberrant tyrosine phosphorylation, which has been linked to the etiology of several human diseases, including cancer. (aacrjournals.org)
  • We previously showed that exposure to metal-laden PM inhibits protein tyrosine phosphatase (PTP) activity in human primary bronchial epithelial cells (HAEC) and leads to Src-dependent activation of EGFR signaling in B82 and A431 cells. (epa.gov)
  • A chemical inhibitor of the EYA tyrosine phosphatase activity inhibited both tumor angiogenesis and tumor growth. (aacrjournals.org)
  • This protein was found to interact with the beta-subunit of Rab geranylgeranyltransferase II (beta GGT II), and thus may function as a regulator of GGT II activity. (antibodies-online.com)
  • The phosphatase activity of PTPN13 is required for this synergism. (biologists.org)
  • 1990) which possess tyrosine phosphatase activity. (springer.com)
  • PTP-PEST is a ubiquitously expressed, cytosolic, mammalian protein tyrosine phosphatase (PTP) which exhibits high specific activity in vitro. (pubmedcentralcanada.ca)
  • Growth cones were found to contain a high level of protein tryrosine phosphatase activity, most of it membrane-associated and forming large, multimeric and wheat germ agglutinin-binding complexes. (biologists.org)
  • Growth cone plating also increased the association with adhesion sites of tyrosine phosphatase activity (14-fold) and of PTPalpha immunoreactivity (6-fold). (biologists.org)
  • This implies a critical role for protein tyrosine phosphatase activity in the earliest phases of adhesion site assembly. (biologists.org)
  • These are the phosphoprotein (serine/threonine) phosphatases (PPases) and the protein tyrosine phosphatases (PTPases). (plantcell.org)
  • This inhibition is also selective for PTP, in that, it has no effect on the serine/threonine phosphatases acid or alkaline phosphatases. (openthesis.org)
  • This book provides coverage, methodology, and laboratory protocols on the more essential aspects of protein tyrosine phosphatase (PTP) function and regulation, including the use of standardized in vitro functional assays, suitable cell systems, and animal and microorganism models. (springer.com)
  • Here, we have described a mechanism of NLRP3 inflammasome regulation by tyrosine phosphorylation of NLRP3 at Tyr861. (jci.org)
  • In: Heilmeyer L.M.G. (eds) Cellular Regulation by Protein Phosphorylation. (springer.com)
  • Pavic K, Duan G, Köhn M (2015) VHR/DUSP3 phosphatase: structure, function and regulation. (springer.com)
  • Cheng A, Uetani N, Simoncic PD, Chaubey VP, Lee-Loy A, McGlade CJ, Kennedy BP, Tremblay ML (2002) Attenuation of leptin action and regulation of obesity by protein tyrosine phosphatase 1B. (springer.com)
  • Of particular interest was the role of protein tyrosine phosphatases in the regulation of Src-cytoskeleton binding. (biologists.org)
  • Protein tyrosine phosphatase 1B negatively regulates integrin signaling. (nih.gov)
  • We recently showed that the receptor protein tyrosine phosphatase μ (PTPμ) negatively regulates GBM cell migration, and full-length PTPμ protein is lost in human GBM tumors in comparison with low-grade astrocytomas ( 8 ). (aacrjournals.org)
  • OBJECTIVE To evaluate safety and efficacy of IONIS-PTP-1B Rx , a second-generation 2′- O -methoxyethyl antisense inhibitor of protein tyrosine phosphatase 1B, as add-on therapy in overweight patients with type 2 diabetes inadequately controlled with metformin with or without sulfonylurea therapy. (diabetesjournals.org)
  • Inhibition of Protein Tyrosine Phosphatase 1B Protects Against Sevoflurane-induced Neurotoxicity mediated by ER stress in Developing Brain. (bioportfolio.com)
  • Hendriks W, Bourgonje A, Leenders W, Pulido R. Proteinaceous Regulators and Inhibitors of Protein Tyrosine Phosphatases. (mdpi.com)
  • This autoinhibition is relieved by binding of the SH2 domains to specific phosphotyrosine sites on receptors or receptor-associated adaptor proteins ( 10 ). (pnas.org)
  • The recombinant AtPTP1 protein specifically hydrolyzed phosphotyrosine, but not phosphoserine/threonine, in protein substrates. (plantcell.org)
  • Accordingly, there are two major groups of phosphatases that remove the phosphate group from phosphoserine/threonine and phosphotyrosine. (plantcell.org)
  • Whereas tyrosine phosphorylation is usually associated with enzyme activation, oxidation leads to PTP inactivation. (ahajournals.org)
  • Receptor tyrosine phosphatases are enzyme-linked receptor phosphatases, a sub-class of protein tyrosine phosphatases. (wikipedia.org)
  • A phytase (myo-inositol hexakisphosphate phosphohydrolase) is any type of phosphatase enzyme that catalyzes the hydrolysis of phytic acid (myo-inositol hexakisphosphate) - an indigestible, organic form of phosphorus that is found in many plant tissues, especially in grains and oil seeds - and releases a usable form of inorganic phosphorus. (wikipedia.org)
  • Most of the known phytases belong to a class of enzyme called histidine acid phosphatases (HAPs). (wikipedia.org)
  • Receptor Protein-Tyrosine Phosphatases (RPTPs) belong to the superfamily of protein-tyrosine phosphatases and have the intrinsic ability to transduce signals across the cell membrane. (nih.gov)
  • In Drosophila, several receptor tyrosine phosphatases (rPTPs), including DLAR, have been shown to participate in directing neurite outgrowth. (biologists.org)
  • It contains an extracellular region composed of 8 fibronectin type-III domains and 3 Ig-like C2-type (immunoglobulin-like) domains, a single transmembrane segment and two tandem intracytoplasmic tyrosine-protein phosphatase domains. (atlasgeneticsoncology.org)
  • The PTPμ extracellular domain is composed of a MAM (meprin/A5-protein/PTPμ) domain, an immunoglobulin-like (Ig) domain, and four fibronectin type III (FNIII) repeats ( 12 , 15 , 16 ). (aacrjournals.org)
  • PTPμ is expressed as a 200-kDa protein that is proteolytically cleaved in the fourth FNIII repeat, resulting in a 100-kDa extracellular fragment (E-subunit) that remains associated with the 100-kDa transmembrane and intracellular portion (P-subunit) through a noncovalent interaction ( 11 , 21 , 22 ). (aacrjournals.org)
  • Chondroitin sulfate proteoglycans (CSPGs) comprise a large family of extracellular matrix glycoproteins with varying numbers and types of glycosaminoglycan (GAG) chains bound to a protein core. (jneurosci.org)
  • Targets include extracellular-regulated kinase 1 and 2 (ERK1/2), stress-activated protein kinase p38 (p38), the Src family tyrosine kinase Fyn, N -methyl- d -aspartate receptors (NMDARs), and α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptors (AMPARs). (aspetjournals.org)
  • In this article, we report that cross-linking the BCR led to a rapid translocation of cytosolic protein tyrosine phosphatase (PTP) 1C to the particulate fraction, where it became associated with a 140-150-kD tyrosyl-phosphorylated protein. (rupress.org)
  • Charest A, Wagner J, Shen SH, Tremblay ML. Murine protein tyrosine phosphatase-PEST, a stable cytosolic protein tyrosine phosphatase. (pubmedcentralcanada.ca)
  • These results suggest that OVA-induced vasocontraction is mediated by the Rho-kinase-dependent inactivation of myosin light chain phosphatase via signaling downstream of Src-induced transactivation of EGFR. (ahajournals.org)
  • Tyrosyl phosphorylation of growth factor receptors via their intrinsic tyrosine kinase activities is a pivotal event for activation of downstream signaling that mediates increased motility and proliferation in cultured cells. (ahajournals.org)
  • ROS influence many signaling events, mainly through oxidative modification of proteins. (ahajournals.org)
  • Human and mouse killer-cell inhibitory receptors recruit PTP1C and PTP1D protein tyrosine phosphatases. (jimmunol.org)
  • NK cells express cell surface receptors for MHC class I proteins (KIR). (jimmunol.org)
  • We demonstrated that protein tyrosine phosphatase non-receptor 22 (PTPN22), variants in which are associated with chronic inflammatory disorders, dephosphorylates NLRP3 upon inflammasome induction, allowing efficient NLRP3 activation and subsequent IL-1β release. (jci.org)
  • The protein tyrosine phosphatase PTPN22( C1858T) allelic polymorphism is associated with increased susceptibility for development of systemic lupus erythematosus (SLE) and other autoimmune diseases. (rupress.org)
  • Specifically, SNPs in immune regulatory genes such as protein tyrosine phosphatase non-receptor type 2 ( PTPN2 ) and PTPN22 ( PTPN2/22 ) could potentially cause these problems in RA. (frontiersin.org)
  • Bottini et al recently found, by a case-control design in two independent populations, a novel association of T1D with a single nucleotide polymorphism (SNP) that caused a R620W aminoacid substitution (dbSNP rs2476601) in the lymphoid protein tyrosine phosphatase, non-receptor type 22 ( PTPN22 ) gene. (bmj.com)
  • 5 PTPN22 encodes LYP, a non-receptor tyrosine phosphatase involved in lymphocyte function. (bmj.com)
  • Recently, an association between a functional R620W polymorphism in protein tyrosine phosphatase PTPN22 and type 1 diabetes has been found by a case-control study. (bmj.com)
  • Downstream from cAMP, protein kinase A (PKA) is probably involved in the maintenance of meiotic arrest. (biologists.org)
  • Protein tyrosine phosphate + H 2 O = protein tyrosine + phosphate. (uniprot.org)
  • and protein tyrosine phosphate + H2O = protein tyrosine + phosphate. (yeastgenome.org)
  • Receptor Tyrosine Phosphatase. (atlasgeneticsoncology.org)
  • The receptor tyrosine phosphatase PTPalpha seems to be the most prevalent species among the membrane-associated enzymes. (biologists.org)
  • Efficient total synthesis of pulchellalactam, a CD45 protein tyrosine phosphatase inhibitor. (sigmaaldrich.com)
  • A new approach to a CD45 protein tyrosine phosphatase inhibitor, pulchellalactam, is described. (sigmaaldrich.com)
  • Charbonneau H, Tonks NK, Walsh, KA, Fischer EH (1988) The leukocyte common antigen (CD45): a putative receptor-linked protein tyrosine phosphatase. (springer.com)
  • Tonks NK, Diltz CD, Fischer EH (1990) CD45, an integral memembrane protein tyrosine phosphatase. (springer.com)
  • Protein-tyrosine-phosphatase that dephosphorylates and probably inhibits MPK6 in non-oxidative stress conditions. (uniprot.org)
  • The protein tyrosine phosphatase (PTP) family is involved in multiple cellular functions and plays an important role in various pathological and physiological processes. (mdpi.com)
  • Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain. (harvard.edu)
  • Protein tyrosine phosphatase (PTP) 1B has long been known to regulate cell proliferation negatively, but the mechanism by which this inhibition occurs is poorly defined. (nih.gov)
  • The PTPRG gene belongs to the receptor class 5 subfamily of the protein-tyrosine phosphatase family. (atlasgeneticsoncology.org)
  • A strong hit in our screen was the tyrosine phosphatase PTPRG. (mcponline.org)
  • SIRT1 improved leptin sensitivity in hypothalamic neurons in vitro and in vivo by downregulating protein-tyrosine phosphatase 1B, T cell protein-tyrosine phosphatase and suppressor of cytokine signalling 3. (curehunter.com)
  • Comparison of the specificity of bacterially expressed cytoplasmic protein-tyrosine phosphatases SHP and SH-PTP2 towards synthetic phosphopeptide substrates. (pubmedcentralcanada.ca)
  • The PPases specifically dephosphorylate phosphoserine/threonine in protein substrates. (plantcell.org)
  • Charbonneau H, Tonks NK, Kumar S, Diltz CD, Harrylock M, Cool DE, Krebs EG, Fischer EH, Walsh KA (1989) Human placenta protein tyrosine phosphatase: Amino acid sequence and relationship to a family of receptor like proteins. (springer.com)
  • We review here recent results on the structure and function of a receptor protein tyrosine phosphatase, RPTPμ. (portlandpress.com)
  • Protein tyrosine phosphatase σ (RPTPσ) has been identified as a critical cognate receptor of CSPGs. (jneurosci.org)
  • It is now well established that the members of the PTP (protein tyrosine phosphatase) superfamily play critical roles in fundamental biological processes. (biochemj.org)
  • The pathway begins with ESCRT-0, a dimer of Vps27 (vacuolar protein sorting 27) and Hse1 [Hrs-binding protein, STAM (signal transducing adaptor molecule) and EAST 1 (EGFR-associated protein with SH3 and TAM domain 1)] [ 13 ]. (biochemsoctrans.org)
  • Isolated from a strain of E. coli that carries a clone expressing the T-Cell protein tyrosine phosphatase under the control of the T7 expression system (kindly provided by Dr. D. Bardford). (neb.com)
  • Proteomic analysis of cisplatin-induced cochlear damage: Methods and early changes in protein expression. (wikigenes.org)
  • In the unlikely event that the protein cannot be expressed or purified we do not charge anything (other companies might charge you for any performed steps in the expression process for custom-made proteins, e.g. fees might apply for the expression plasmid, the first expression experiments or purification optimization). (antibodies-online.com)
  • Cool DE, Tonks NH, Charbonneau H, Fischer EH, Krebs EG (1990) Expression of a human T-cell protein-tyrosine-phosphatase in baby hamster kidney cells. (springer.com)
  • Guan KL, Haun RS, Watson SJ, Gaehlen RL, Dixon JE (1990) Cloning and expression of a protein tyrosine phosphatase. (springer.com)
  • He RJ, Yu ZH, Zhang RY, Zhang ZY (2014) Protein tyrosine phosphatases as potential therapeutic targets. (springer.com)
  • These results document a common pathway by which diverse KIR can down-regulate NK and T cell activation programs, and further define the sequence of the immunoreceptor tyrosine-based inhibitory motif (ITIM), initially described in FcgammaRIIB1, and expressed in both human and mouse KIR. (jimmunol.org)
  • Single-pass type I membrane protein. (atlasgeneticsoncology.org)
  • This cleavage primes PTPκ PΔE to be cleaved by γ-secretase, which releases the intracellular portion of PTPκ containing the active phosphatase domain from the membrane ( 23 ). (aacrjournals.org)
  • Phase separation of protein homogenates by Triton X-114 extraction indicated that this triplet was enriched in soluble but not membrane fractions. (jneurosci.org)
  • Plasma membrane proteins govern how cells sense their environment, and therefore, the surface levels of many of these proteins are subject to strict control. (biochemsoctrans.org)
  • A key device for exerting such control is the endocytic pathway, and of particular importance is determining the fate of internalised membrane proteins once they enter the early endosome. (biochemsoctrans.org)
  • Internalised plasma membrane proteins either recycle or are ubiquitinated and sorted to the MVB. (biochemsoctrans.org)
  • ESCRT complexes act in succession to facilitate the MVB sorting of ubiquitinated membrane proteins. (biochemsoctrans.org)
  • It thus encodes a protein that lacks a 411 aa internal fragment, and has one amino acid change, as compared to isoform 1 and is 8845 bp in length (Figure B). (atlasgeneticsoncology.org)
  • The nontransmembrane tyrosine phosphatase PTP-1B localizes to the endoplasmic reticulum via its 35 amino acid C-terminal sequence. (pubmedcentralcanada.ca)
  • Recombinant human PTP4A2 protein, fused to His-tag at N-terminus, was expressed in E.coli and purified by using conventional chromatography techniques. (antibodies-online.com)