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)
An enzyme that deactivates glycogen phosphorylase a by releasing inorganic phosphate and phosphorylase b, the inactive form. EC 3.1.3.17.
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.
A group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
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.
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)
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
A family of enzymes that catalyze the conversion of ATP and a protein to ADP and a phosphoprotein.
A compound that, along with its isomer, Cleland's reagent (DITHIOTHREITOL), is used for the protection of sulfhydryl groups against oxidation to disulfides and for the reduction of disulfides to sulfhydryl groups.
Compounds of the general formula R-O-R arranged in a ring or crown formation.
A trace element with atomic symbol Mn, atomic number 25, and atomic weight 54.94. It is concentrated in cell mitochondria, mostly in the pituitary gland, liver, pancreas, kidney, and bone, influences the synthesis of mucopolysaccharides, stimulates hepatic synthesis of cholesterol and fatty acids, and is a cofactor in many enzymes, including arginase and alkaline phosphatase in the liver. (From AMA Drug Evaluations Annual 1992, p2035)
An enzyme that catalyzes the conversion of an orthophosphoric monoester and water to an alcohol and orthophosphate. EC 3.1.3.2.
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 trihydroxy bile salt that is used as a digestive aid in dietary supplements. It is used in culture media and in conjunction with PAPAIN and PANCREATIN.
The rate dynamics in chemical or physical systems.
The sum of the weight of all the atoms in a molecule.
A class of glucosyltransferases that catalyzes the degradation of storage polysaccharides, such as glucose polymers, by phosphorolysis in animals (GLYCOGEN PHOSPHORYLASE) and in plants (STARCH PHOSPHORYLASE).
A toxic compound, isolated from the Spanish fly or blistering beetle (Lytta (Cantharis) vesicatoria) and other insects. It is a potent and specific inhibitor of protein phosphatases 1 (PP1) and 2A (PP2A). This compound can produce severe skin inflammation, and is extremely toxic if ingested orally.
Proteins which bind calmodulin. They are found in many tissues and have a variety of functions including F-actin cross-linking properties, inhibition of cyclic nucleotide phosphodiesterase and calcium and magnesium ATPases.
Five-membered heterocyclic ring structures containing an oxygen in the 1-position and a nitrogen in the 3-position, in distinction from ISOXAZOLES where they are at the 1,2 positions.
Unstable isotopes of phosphorus that decay or disintegrate emitting radiation. P atoms with atomic weights 28-34 except 31 are radioactive phosphorus isotopes.
A source of inorganic fluoride which is used topically to prevent dental caries.
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.
A metallic element that has the atomic symbol Mg, atomic number 12, and atomic weight 24.31. It is important for the activity of many enzymes, especially those involved in OXIDATIVE PHOSPHORYLATION.
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.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
A phosphoprotein that was initially identified as a major target of DOPAMINE activated ADENYLYL CYCLASE in the CORPUS STRIATUM. It regulates the activities of PROTEIN PHOSPHATASE-1 and PROTEIN KINASE A, and it is a key mediator of the biochemical, electrophysiological, transcriptional, and behavioral effects of DOPAMINE.
The species Oryctolagus cuniculus, in the family Leporidae, order LAGOMORPHA. Rabbits are born in burrows, furless, and with eyes and ears closed. In contrast with HARES, rabbits have 22 chromosome pairs.
Domesticated bovine animals of the genus Bos, usually kept on a farm or ranch and used for the production of meat or dairy products or for heavy labor.
An adenine nucleotide containing three phosphate groups esterified to the sugar moiety. In addition to its crucial roles in metabolism adenosine triphosphate is a neurotransmitter.
A CALCIUM and CALMODULIN-dependent serine/threonine protein phosphatase that is composed of the calcineurin A catalytic subunit and the calcineurin B regulatory subunit. Calcineurin has been shown to dephosphorylate a number of phosphoproteins including HISTONES; MYOSIN LIGHT CHAIN; and the regulatory subunits of CAMP-DEPENDENT PROTEIN KINASES. It is involved in the regulation of signal transduction and is the target of an important class of immunophilin-immunosuppressive drug complexes.
An enzyme that catalyzes the conversion of ATP and PHOSPHORYLASE B to ADP and PHOSPHORYLASE A.
Contractile tissue that produces movement in animals.
A phenothiazine with actions similar to CHLORPROMAZINE. It is used as an antipsychotic and an antiemetic.
The chemical and physical integrity of a pharmaceutical product.
An adenine nucleotide containing one phosphate group which is esterified to both the 3'- and 5'-positions of the sugar moiety. It is a second messenger and a key intracellular regulator, functioning as a mediator of activity for a number of hormones, including epinephrine, glucagon, and ACTH.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Compounds and molecular complexes that consist of very large numbers of atoms and are generally over 500 kDa in size. In biological systems macromolecular substances usually can be visualized using ELECTRON MICROSCOPY and are distinguished from ORGANELLES by the lack of a membrane structure.
An enzyme that catalyzes the conversion of D-glucose 6-phosphate and water to D-glucose and orthophosphate. EC 3.1.3.9.
Enzymes that catalyze the reversible reduction of alpha-carboxyl group of 3-hydroxy-3-methylglutaryl-coenzyme A to yield MEVALONIC ACID.
A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances.
Intracellular fluid from the cytoplasm after removal of ORGANELLES and other insoluble cytoplasmic components.
A heat-stable, low-molecular-weight activator protein found mainly in the brain and heart. The binding of calcium ions to this protein allows this protein to bind to cyclic nucleotide phosphodiesterases and to adenyl cyclase with subsequent activation. Thereby this protein modulates cyclic AMP and cyclic GMP levels.
Compounds or agents that combine with an enzyme in such a manner as to prevent the normal substrate-enzyme combination and the catalytic reaction.
Small chromosomal proteins (approx 12-20 kD) possessing an open, unfolded structure and attached to the DNA in cell nuclei by ionic linkages. Classification into the various types (designated histone I, histone II, etc.) is based on the relative amounts of arginine and lysine in each.
The normality of a solution with respect to HYDROGEN ions; H+. It is related to acidity measurements in most cases by pH = log 1/2[1/(H+)], where (H+) is the hydrogen ion concentration in gram equivalents per liter of solution. (McGraw-Hill Dictionary of Scientific and Technical Terms, 6th ed)
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.
Presence of warmth or heat or a temperature notably higher than an accustomed norm.
Genetically identical individuals developed from brother and sister matings which have been carried out for twenty or more generations or by parent x offspring matings carried out with certain restrictions. This also includes animals with a long history of closed colony breeding.
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 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.
A subclass of dual specificity phosphatases that play a role in the progression of the CELL CYCLE. They dephosphorylate and activate CYCLIN-DEPENDENT KINASES.
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 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 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 part of CENTRAL NERVOUS SYSTEM that is contained within the skull (CRANIUM). Arising from the NEURAL TUBE, the embryonic brain is comprised of three major parts including PROSENCEPHALON (the forebrain); MESENCEPHALON (the midbrain); and RHOMBENCEPHALON (the hindbrain). The developed brain consists of CEREBRUM; CEREBELLUM; and other structures in the BRAIN STEM.
The muscle tissue of the HEART. It is composed of striated, involuntary muscle cells (MYOCYTES, CARDIAC) connected to form the contractile pump to generate blood flow.
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 subcategory of protein tyrosine phosphatases that occur in the CYTOPLASM. Many of the proteins in this category play a role in intracellular signal transduction.
Established cell cultures that have the potential to propagate indefinitely.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Monomeric subunits of primarily globular ACTIN and found in the cytoplasmic matrix of almost all cells. They are often associated with microtubules and may play a role in cytoskeletal function and/or mediate movement of the cell or the organelles within the cell.
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.
A phosphomonoesterase involved in the synthesis of triacylglycerols. It catalyzes the hydrolysis of phosphatidates with the formation of diacylglycerols and orthophosphate. EC 3.1.3.4.
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.
The phosphoric acid ester of serine.
The phosphoric acid ester of threonine. Used as an identifier in the analysis of peptides, proteins, and enzymes.
Inorganic salts of phosphoric acid.
A family of synaptic vesicle-associated proteins involved in the short-term regulation of NEUROTRANSMITTER release. Synapsin I, the predominant member of this family, links SYNAPTIC VESICLES to ACTIN FILAMENTS in the presynaptic nerve terminal. These interactions are modulated by the reversible PHOSPHORYLATION of synapsin I through various signal transduction pathways. The protein is also a substrate for cAMP- and CALCIUM-CALMODULIN-DEPENDENT PROTEIN KINASES. It is believed that these functional properties are also shared by synapsin II.
A non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
A subclass of receptor-like protein tryosine phosphatases that contain a single cytosolic protein tyrosine phosphate domain and multiple extracellular fibronectin III-like domains.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
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.
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 short highly glycosylated extracellular domains and two active cytosolic protein tyrosine phosphatase domains.
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 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 subcategory of phosphohydrolases that are specific for MITOGEN-ACTIVATED PROTEIN KINASES. They play a role in the inactivation of the MAP KINASE SIGNALING SYSTEM.
Proteins found in any species of virus.
A ubiquitous phosphoprotein that serves as an intracellular substrate for a variety of SIGNAL TRANSDUCTION PATHWAYS. PHOSPHORYLATION of stathmin occurs during CELL CYCLE progression, and stathmin functions as a microtubule-destabilizing protein that promotes MICROTUBULE depolymerization during INTERPHASE and late MITOSIS. Stathmin is expressed at very high levels in a variety of human CANCERS.
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 parts of a macromolecule that directly participate in its specific combination with another molecule.
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.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
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.
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.
Proteins prepared by recombinant DNA technology.
Analysis of PEPTIDES that are generated from the digestion or fragmentation of a protein or mixture of PROTEINS, by ELECTROPHORESIS; CHROMATOGRAPHY; or MASS SPECTROMETRY. The resulting peptide fingerprints are analyzed for a variety of purposes including the identification of the proteins in a sample, GENETIC POLYMORPHISMS, patterns of gene expression, and patterns diagnostic for diseases.
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 and is primarily localized to the CYTOSOL.
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.
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.
An egg yolk phosphoglycoprotein which contains about 90% of the yolk protein phosphorus. It is synthesized in the liver of the hen and transferred to the developing oocyte, where it is bound to lipoproteins within the yolk granules.
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.
Electrophoresis in which a second perpendicular electrophoretic transport is performed on the separate components resulting from the first electrophoresis. This technique is usually performed on polyacrylamide gels.
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.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
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.
Cyclic heptapeptides found in MICROCYSTIS and other CYANOBACTERIA. Hepatotoxic and carcinogenic effects have been noted. They are sometimes called cyanotoxins, which should not be confused with chemicals containing a cyano group (CN) which are toxic.
A negatively-charged extracellular matrix protein that plays a role in the regulation of BONE metabolism and a variety of other biological functions. Cell signaling by osteopontin may occur through a cell adhesion sequence that recognizes INTEGRIN ALPHA-V BETA-3.
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.
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.
Proteins found in the nucleus of a cell. Do not confuse with NUCLEOPROTEINS which are proteins conjugated with nucleic acids, that are not necessarily present in the nucleus.
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.
Within a eukaryotic cell, a membrane-limited body which contains chromosomes and one or more nucleoli (CELL NUCLEOLUS). The nuclear membrane consists of a double unit-type membrane which is perforated by a number of pores; the outermost membrane is continuous with the ENDOPLASMIC RETICULUM. A cell may contain more than one nucleus. (From Singleton & Sainsbury, Dictionary of Microbiology and Molecular Biology, 2d ed)
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.
Proteins found in the microtubules.
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.
An essential amino acid occurring naturally in the L-form, which is the active form. It is found in eggs, milk, gelatin, and other proteins.
An enzyme that catalyzes the conversion of phosphorylated, inactive glycogen synthase D to active dephosphoglycogen synthase I. EC 3.1.3.42.
Transport proteins that carry specific substances in the blood or across cell membranes.
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.
Components of a cell produced by various separation techniques which, though they disrupt the delicate anatomy of a cell, preserve the structure and physiology of its functioning constituents for biochemical and ultrastructural analysis. (From Alberts et al., Molecular Biology of the Cell, 2d ed, p163)
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
A group of enzymes that are dependent on CYCLIC AMP and catalyze the phosphorylation of SERINE or THREONINE residues on proteins. Included under this category are two cyclic-AMP-dependent protein kinase subtypes, each of which is defined by its subunit composition.
Glycoproteins which contain sialic acid as one of their carbohydrates. They are often found on or in the cell or tissue membranes and participate in a variety of biological activities.
A subclass of receptor-like protein tryosine phosphatases that contain an extracellular fibronectin III-like domain along with a carbonic anhydrase-like domain.
(Pyruvate dehydrogenase (lipoamide))-phosphate phosphohydrolase. A mitochondrial enzyme that catalyzes the hydrolytic removal of a phosphate on a specific seryl hydroxyl group of pyruvate dehydrogenase, reactivating the enzyme complex. EC 3.1.3.43.
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.
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 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.
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).)
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.
A ubiquitous casein kinase that is comprised of two distinct catalytic subunits and dimeric regulatory subunit. Casein kinase II has been shown to phosphorylate a large number of substrates, many of which are proteins involved in the regulation of gene expression.
The region of an enzyme that interacts with its substrate to cause the enzymatic reaction.
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
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.
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.
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.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
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.
A type of CELL NUCLEUS division by means of which the two daughter nuclei normally receive identical complements of the number of CHROMOSOMES of the somatic cells of the species.
A species of the genus SACCHAROMYCES, family Saccharomycetaceae, order Saccharomycetales, known as "baker's" or "brewer's" yeast. The dried form is used as a dietary supplement.
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.
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.
A specialized CONNECTIVE TISSUE that is the main constituent of the SKELETON. The principle cellular component of bone is comprised of OSTEOBLASTS; OSTEOCYTES; and OSTEOCLASTS, while FIBRILLAR COLLAGENS and hydroxyapatite crystals form the BONE MATRIX.
Elements of limited time intervals, contributing to particular results or situations.
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.
Proteins conjugated with nucleic acids.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in enzyme synthesis.
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)
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 species of gram-negative, facultatively anaerobic, rod-shaped bacteria (GRAM-NEGATIVE FACULTATIVELY ANAEROBIC RODS) commonly found in the lower part of the intestine of warm-blooded animals. It is usually nonpathogenic, but some strains are known to produce DIARRHEA and pyogenic infections. Pathogenic strains (virotypes) are classified by their specific pathogenic mechanisms such as toxins (ENTEROTOXIGENIC ESCHERICHIA COLI), etc.
The type species of LYSSAVIRUS causing rabies in humans and other animals. Transmission is mostly by animal bites through saliva. The virus is neurotropic multiplying in neurons and myotubes of vertebrates.
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.
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
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.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Separation technique in which the stationary phase consists of ion exchange resins. The resins contain loosely held small ions that easily exchange places with other small ions of like charge present in solutions washed over the resins.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
An enzyme that catalyzes the hydrolysis of nitrophenyl phosphates to nitrophenols. At acid pH it is probably ACID PHOSPHATASE (EC 3.1.3.2); at alkaline pH it is probably ALKALINE PHOSPHATASE (EC 3.1.3.1). EC 3.1.3.41.
Chromatography on non-ionic gels without regard to the mechanism of solute discrimination.

Inducible NO synthase: role in cellular signalling. (1/5093)

The discovery of endothelium-derived relaxing factor and its identification as nitric oxide (NO) was one of the most exciting discoveries of biomedical research in the 1980s. Besides its potent vasodilatory effects, NO was found under certain circumstances to be responsible for the killing of microorganisms and tumour cells by activated macrophages and to act as a novel, unconventional type of neurotransmitter. In 1992, Science picked NO as the 'Molecule of the Year', and over the past years NO has become established as a universal intercellular messenger that acutely affects important signalling pathways and, on a more long-term scale, modulates gene expression in target cells. These actions will form the focus of the present review.  (+info)

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. (2/5093)

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)

The MAP kinase ERK2 inhibits the cyclic AMP-specific phosphodiesterase HSPDE4D3 by phosphorylating it at Ser579. (3/5093)

The extracellular receptor stimulated kinase ERK2 (p42(MAPK))-phosphorylated human cAMP-specific phosphodiesterase PDE4D3 at Ser579 and profoundly reduced ( approximately 75%) its activity. These effects could be reversed by the action of protein phosphatase PP1. The inhibitory state of PDE4D3, engendered by ERK2 phosphorylation, was mimicked by the Ser579-->Asp mutant form of PDE4D3. In COS1 cells transfected to express PDE4D3, challenge with epidermal growth factor (EGF) caused the phosphorylation and inhibition of PDE4D3. This effect was blocked by the MEK inhibitor PD98059 and was not apparent using the Ser579-->Ala mutant form of PDE4D3. Challenge of HEK293 and F442A cells with EGF led to the PD98059-ablatable inhibition of endogenous PDE4D3 and PDE4D5 activities. EGF challenge of COS1 cells transfected to express PDE4D3 increased cAMP levels through a process ablated by PD98059. The activity of the Ser579-->Asp mutant form of PDE4D3 was increased by PKA phosphorylation. The transient form of the EGF-induced inhibition of PDE4D3 is thus suggested to be due to feedback regulation by PKA causing the ablation of the ERK2-induced inhibition of PDE4D3. We identify a novel means of cross-talk between the cAMP and ERK signalling pathways whereby cell stimuli that lead to ERK2 activation may modulate cAMP signalling.  (+info)

All-trans-retinoic acid inhibits Jun N-terminal kinase by increasing dual-specificity phosphatase activity. (4/5093)

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)

The yeast ser/thr phosphatases sit4 and ppz1 play opposite roles in regulation of the cell cycle. (5/5093)

Yeast cells overexpressing the Ser/Thr protein phosphatase Ppz1 display a slow-growth phenotype. These cells recover slowly from alpha-factor or nutrient depletion-induced G1 arrest, showing a considerable delay in bud emergence as well as in the expression of the G1 cyclins Cln2 and Clb5. Therefore, an excess of the Ppz1 phosphatase interferes with the normal transition from G1 to S phase. The growth defect is rescued by overexpression of the HAL3/SIS2 gene, encoding a negative regulator of Ppz1. High-copy-number expression of HAL3/SIS2 has been reported to improve cell growth and to increase expression of G1 cyclins in sit4 phosphatase mutants. We show here that the described effects of HAL3/SIS2 on sit4 mutants are fully mediated by the Ppz1 phosphatase. The growth defect caused by overexpression of PPZ1 is intensified in strains with low G1 cyclin levels (such as bck2Delta or cln3Delta mutants), whereas mutation of PPZ1 rescues the synthetic lethal phenotype of sit4 cln3 mutants. These results reveal a role for Ppz1 as a regulatory component of the yeast cell cycle, reinforce the notion that Hal3/Sis2 serves as a negative modulator of the biological functions of Ppz1, and indicate that the Sit4 and Ppz1 Ser/Thr phosphatases play opposite roles in control of the G1/S transition.  (+info)

Purification and identification of a novel subunit of protein serine/threonine phosphatase 4. (6/5093)

The catalytic subunit of protein serine/threonine phosphatase 4 (PP4C) has greater than 65% amino acid identity to the catalytic subunit of protein phosphatase 2A (PP2AC). Despite this high homology, PP4 does not appear to associate with known PP2A regulatory subunits. As a first step toward characterization of PP4 holoenzymes and identification of putative PP4 regulatory subunits, PP4 was purified from bovine testis soluble extracts. PP4 existed in two complexes of approximately 270-300 and 400-450 kDa as determined by gel filtration chromatography. The smaller PP4 complex was purified by sequential phenyl-Sepharose, Source 15Q, DEAE2, and Superdex 200 gel filtration chromatographies. The final product contained two major proteins: the PP4 catalytic subunit plus a protein that migrated as a doublet of 120-125 kDa on SDS-polyacrylamide gel electrophoresis. The associated protein, termed PP4R1, and PP4C also bound to microcystin-Sepharose. Mass spectrometry analysis of the purified complex revealed two major peaks, at 35 (PP4C) and 105 kDa (PP4R1). Amino acid sequence information of several peptides derived from the 105 kDa protein was utilized to isolate a human cDNA clone. Analysis of the predicted amino acid sequence revealed 13 nonidentical repeats similar to repeats found in the A subunit of PP2A (PP2AA). The PP4R1 cDNA clone engineered with an N-terminal Myc tag was expressed in COS M6 cells and PP4C co-immunoprecipitated with Myc-tagged PP4R1. These data indicate that one form of PP4 is similar to the core complex of PP2A in that it consists of a catalytic subunit and a "PP2AA-like" structural subunit.  (+info)

Caffeine can override the S-M checkpoint in fission yeast. (7/5093)

The replication checkpoint (or 'S-M checkpoint') control prevents progression into mitosis when DNA replication is incomplete. Caffeine has been known for some time to have the capacity to override the S-M checkpoint in animal cells. We show here that caffeine also disrupts the S-M checkpoint in the fission yeast Schizosaccharomyces pombe. By contrast, no comparable effects of caffeine on the S. pombe DNA damage checkpoint were seen. S. pombe cells arrested in early S phase and then exposed to caffeine lost viability rapidly as they attempted to enter mitosis, which was accompanied by tyrosine dephosphorylation of Cdc2. Despite this, the caffeine-induced loss of viability was not blocked in a temperature-sensitive cdc2 mutant incubated at the restrictive temperature, although catastrophic mitosis was prevented under these conditions. This suggests that, in addition to S-M checkpoint control, a caffeine-sensitive function may be important for maintenance of cell viability during S phase arrest. The lethality of a combination of caffeine with the DNA replication inhibitor hydroxyurea was suppressed by overexpression of Cds1 or Chk1, protein kinases previously implicated in S-M checkpoint control and recovery from S phase arrest. In addition, the same combination of drugs was specifically tolerated in cells overexpressing either of two novel S. pombe genes isolated in a cDNA library screen. These findings should allow further molecular investigation of the regulation of S phase arrest, and may provide a useful system with which to identify novel drugs that specifically abrogate the checkpoint control.  (+info)

Activation of myosin phosphatase targeting subunit by mitosis-specific phosphorylation. (8/5093)

It has been demonstrated previously that during mitosis the sites of myosin phosphorylation are switched between the inhibitory sites, Ser 1/2, and the activation sites, Ser 19/Thr 18 (Yamakita, Y., S. Yamashiro, and F. Matsumura. 1994. J. Cell Biol. 124:129- 137; Satterwhite, L.L., M.J. Lohka, K.L. Wilson, T.Y. Scherson, L.J. Cisek, J.L. Corden, and T.D. Pollard. 1992. J. Cell Biol. 118:595-605), suggesting a regulatory role of myosin phosphorylation in cell division. To explore the function of myosin phosphatase in cell division, the possibility that myosin phosphatase activity may be altered during cell division was examined. We have found that the myosin phosphatase targeting subunit (MYPT) undergoes mitosis-specific phosphorylation and that the phosphorylation is reversed during cytokinesis. MYPT phosphorylated either in vivo or in vitro in the mitosis-specific way showed higher binding to myosin II (two- to threefold) compared to MYPT from cells in interphase. Furthermore, the activity of myosin phosphatase was increased more than twice and it is suggested this reflected the increased affinity of myosin binding. These results indicate the presence of a unique positive regulatory mechanism for myosin phosphatase in cell division. The activation of myosin phosphatase during mitosis would enhance dephosphorylation of the myosin regulatory light chain, thereby leading to the disassembly of stress fibers during prophase. The mitosis-specific effect of phosphorylation is lost on exit from mitosis, and the resultant increase in myosin phosphorylation may act as a signal to activate cytokinesis.  (+info)

Growth factor receptor levels are aberrantly high in diverse cancers, driving the proliferation and survival of tumor cells. Understanding the molecular basis for this aberrant elevation has profound clinical implications. Here we show that the pleckstrin homology domain leucine-rich repeat protein phosphatase (PHLPP) suppresses receptor tyrosine kinase (RTK) signaling output by a previously unidentified epigenetic mechanism unrelated to its previously described function as the hydrophobic motif phosphatase for the protein kinase AKT, protein kinase C, and S6 kinase. Specifically, we show that nuclear-localized PHLPP suppresses histone phosphorylation and acetylation, in turn suppressing the transcription of diverse growth factor receptors, including the EGF receptor. These data uncover a much broader role for PHLPP in regulation of growth factor signaling beyond its direct inactivation of AKT: By suppressing RTK levels, PHLPP dampens the downstream signaling output of two major oncogenic pathways, the
The dephosphorylation of the modulator subunit is an essential step in the kinase FA-mediated activation of the ATP,Mg-dependent protein phosphatase. Mg2+ is implicated in this autocatalytic dephosphorylation which is not effected by the addition of phosphoinhibitor-1. Dephosphorylation of free modulator by the catalytic subunit is also largely Mg2+-dependent but can be abolished by phosphoinhibitor-1 in concentrations comparable to the amount of modulator used as substrate (micromolar). The phosphorylase phosphatase activity of the catalytic subunit is inhibited by nanomolar concentrations of phosphoinhibitor-1 and is completely independent of divalent cations ...
Protein serine/threonine phosphatase (PSP)[1] is a form of phosphoprotein phosphatase that acts upon phosphorylated serine/threonine residues. Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate to reverse the regulation signal. Ser/Thr-specific protein phosphatases are regulated partly by their location within the cell and by specific inhibitor proteins. Serine and threonine are amino acids which have similar side-chain compositions that contain a hydroxyl group and thus can be phosphorylated by enzymes called serine/threonine protein kinases. The addition of the phosphate group can be reversed by enzymes called serine/threonine phosphatases. The addition and removal of phosphate groups regulates many cellular pathways involved in cell proliferation, programmed cell death (apoptosis), embryonic development, and cell differentiation. ...
Paclitaxel and docetaxel (taxoids) are chemotherapy agents whose mode of action is through an effect on cellular microtubules. Several studies have investigated their potential in the treatment of myeloid malignancies. The aim of our study was to investigate the potential role of the serine/threonine protein phosphatase system in docetaxel/paclitaxel induced cytotoxicity on HL 60 cells. The IC50 dose of paclitaxel and docetaxel were found as 20 and 5 nM respectively using trypan blue dye exclusion and XTT assays. Treating HL 60 cells with docetaxel and paclitaxel resulted in dose and time dependent cytotoxicity. Docetaxel induced the decrease in the activity of protein phosphatase 1 (PP1) and increase in the activity of PP2 subgroups, while paclitaxel induced the increase in the activity of PP1 and decrease in the activity of PP2 subgroups. Potential use of specific protein phosphatase inhibitors or activators in combination with taxoids will open new windows in the treatment of myeloid ...
Calyculins, highly cytotoxic polyketides, originally isolated from the marine sponge Discodermia calyx by Fusetani and co-workers, belong to the lithistid sponges group. These molecules have become interesting targets for cell biologists and synthetic organic chemists. The serine/threonine protein phosphatases play an essential role in the cellular signalling, metabolism, and cell cycle control. Calyculins express potent protein phosphatase 1 and 2A inhibitory activity, and have therefore become valuable tools for cellular biologists studying intracellular processes and their control by reversible phosphorylation. Calyculins might also play an important role in the development of several diseases such as cancer, neurodegenerative diseases, and type 2-diabetes mellitus. The fascinating structures of calyculins have inspired various groups of synthetic organic chemists to develop total syntheses of the most abundant calyculins A and C. However, with fifteen chiral centres, a cyano-capped tetraene unit, a
MW 721.83, Purity | 98%. Mycotoxin and protein serine/threonine phosphatase inhibitor (IC50 values are 80 μM (PP5), 0.3 (PP2Cα), 0.4 ( PP2A), 0.5 (PP1γ2) and 3 mM (PP2B)). Cell proliferation…
plasma membrane, magnesium-dependent protein serine/threonine phosphatase activity, protein serine/threonine phosphatase activity, drought recovery, microtubule cytoskeleton organization, negative regulation of growth, protein dephosphorylation
plasma membrane, magnesium-dependent protein serine/threonine phosphatase activity, protein serine/threonine phosphatase activity
Title: In-Gel Protein Phosphatase Assays and Other Useful Methods for the Detection of Protein Phosphatase Activities. VOLUME: 11 ISSUE: 1. Author(s):Atsuhiko Ishida and Isamu Kameshita. Affiliation:Laboratory of Molecular Brain Science, Graduate School of Integrated Arts and Sciences, Hiroshima University, 1-7-1 Kagamiyama, Higashi-Hiroshima 739-8521, Japan.. Keywords:Electrophoresis, fluorescence, in-gel assay, peptide conjugate, phosphatase activity, serine/threonine phosphatase, synthetic phosphopeptide, tyrosine phosphatase, DUSPs, MKPs, VacA. Abstract: Intracellular signaling is governed by protein phosphorylation and dephosphorylation catalyzed by protein kinases and protein phosphatases, respectively. Since there is growing evidence that a variety of protein phosphatases are involved in the pathogenesis of various diseases, protein phosphatases have recently been the focus of intense research interest, not only in basic biology but also in clinical medicine. In the process of these ...
TY - JOUR. T1 - The PPZ protein phosphatases are important determinants of salt tolerance in yeast cells. AU - Posas, F.. AU - Camps, M.. AU - Arino, J.. PY - 1995/1/1. Y1 - 1995/1/1. N2 - Protein phosphatases PPZ1 and PPZ2 represent a novel form of Ser/Thr phosphatases structurally related to type 1 phosphatases and characterized by an unusual amino-terminal region. We have found that the deletion of PPZ1 gene results in increased tolerance to Na+ and Li+ cations. Simultaneous deletion of PPZ2 gene results in an additional increase in salt tolerance. After exposure to high concentration of Li+, the intracellular content of the cation was markedly decreased in ppz1Δ ppz2Δ mutants when compared to wild type cells. No significant differences were observed between both strains when the Li+ influx was measured, but ppz1Δ ppz2Δ mutants eliminated Li+ more efficiently than wild type cells. This can be explained by the fact that expression of the ENA1 gene, which encodes the major component of the ...
TY - JOUR. T1 - A heterozygous deficiency in protein phosphatase Ppm1b results in an altered ovulation number in mice. AU - Ishii, Naoki. AU - Homma, Takujiro. AU - Watanabe, Ren. AU - Kimura, Naoko. AU - Ohnishi, Motoko. AU - Kobayashi, Takayasu. AU - Fujii, Junichi. N1 - Funding Information: This work was partly supported by the cooperative research Project Program of the Joint usage/research center at the institute of development, aging and cancer, Tohoku university (grant no. 2012-4).. PY - 2019. Y1 - 2019. N2 - Ppm1b, a metal-dependent serine/threonine protein phosphatase, catalyzes the dephosphorylation of a variety of phosphorylated proteins. Ppm1b-/- mouse embryos die at the fertilized oocyte stage, whereas Ppm1b+/- mice with a c57Bl/6 background exhibit no phenotypic abnormalities. Because the c57Bl/6 strain produces a limited number of pups, in an attempt to produce Ppm1b-/- mice, congenic Ppm1b+/- mice with an icr background were established, which are more fertile and gave birth to ...
EC 3.1.3.16; recommended name: phosphoprotein phosphatase; other names: protein phosphatase‐1; protein phosphatase‐2A; protein phosphatase‐2B; protein phosphatase‐2C. This name includes enzymes that hydrolyse the serine‐ or threonine‐bound phosphate group from phosphoproteins.. [...] ...
TY - JOUR. T1 - Cloning, Expression, and Catalytic Mechanism of the Low Molecular Weight Phosphotyrosyl Protein Phosphatase from Bovine Heart. AU - Wo, Yu Yuan P.. AU - Zhou, Ming Ming. AU - Stevis, Panayiotis. AU - Davis, June P.. AU - Zhang, Zhong Yin. AU - Van Etten, Robert L.. PY - 1992/2/1. Y1 - 1992/2/1. N2 - The first representative of a group of mammalian, low molecular weight phosphotyrosyl protein phosphatases was cloned, sequenced and expressed in Escherichia coli. Using a 61-mer oligonucleotide probe based on the amino acid sequence of the purified enzyme, several overlapping cDNA clones were isolated from a bovine heart cDNA library. A full-length clone was obtained consisting of a 27-bp 5ʹ3ʹ noncoding region, an open reading frame encoding the expected 157 amino acid protein, and an extensive 3 nontranslated sequence. The identification of the clone as full length was consistent with results obtained in mRNA blotting experiments using poly(A)+ mRNA from bovine heart. The coding ...
Supplementary MaterialsSupplementary Table 1. prolonged lifespan of was associated with decreased levels of daf-16 which related to the insulin/insulin-like growth factor signaling pathway (IIS) activity and reactive air types (ROS), whereas heat surprise transcription aspect-1 (hsf-1) pathway had not been … Continue reading →. ...
Supplementary MaterialsSupplementary Table 1: Venn diagram list in term and preterm labor cerm-2019-03013-suppl1. in placentas with swelling. We also proven that many miRNAs (miR-371a-5p, miR-3065-3p, miR-519b-3p, and miR-373-3p) straight targeted their focus on genes (and had not been modified by LPS treatment. Summary These results offer applicant miRNAs and their focus on genes that may be Ganetespib price utilized as placental biomarkers of swelling. These applicants may be helpful for additional miRNA-based biomarker development. research. The cells had been taken care of at 37C in 5% CO2. The tradition moderate was RPMI-1640 (Gibco, Grand Isle, NY, USA) supplemented with 5% fetal bovine serum (FBS; Gibco) and 1% penicillin-streptomycin (Gibco). HeLa cells (a cervical tumor cell range) had been cultured with Dulbeccos customized Eagle medium (Gibco) containing 5% FBS (Gibco) and 1% penicillin-streptomycin (Gibco). 3. Lipopolysaccharide treatment and miRNA transfection The HTR-8/SVneo ...
The Saccharomyces Genome Database (SGD) provides comprehensive integrated biological information for the budding yeast Saccharomyces cerevisiae.
The catalytic subunit of type 1 protein phosphatase (PP1C) interacts with a large number of polypeptides in eukaryotic cells from yeast to man and these regulatory subunits can both modulate the activ
Phosphoprotein phosphatases, which hydrolyze the phosphoester bonds of phosphoserines, phosphothreonines or phosphotyrosines, play an essential role in signal transduction and actively contribute to the regulation of protein phosphorylation. On the basis of their substrate specificity they are usually divided into phosphoserine and phosphothreonine phosphatases on the one hand, and phosphotyrosine and dual-specificity phosphatases, on the other hand. This division corresponds also to different families of enzymes with different catalytic mechanisms. Genes coding for phosphoserine/threonine phosphatases are less numerous in vertebrate genomes than those for serine /threonine kinases, and the complexity of phosphatases function arises in part from the interactions of catalytic subunits with other proteins.. Prior to the knowledge of their sequence, phosphoserine/threonine phosphatases were classified on the basis of their substrate preference and inhibitor sensitivity. Type 1 protein phosphatases ...
A protein phosphatase was cloned that interacts with a serine-threonine receptor-like kinase, RLK5, from Arabidopsis thaliana. The phosphatase, designated KAPP (kinase-associated protein phosphatase), is composed of three domains: an amino-terminal signal anchor, a kinase interaction (KI) domain, and a type 2C protein phosphatase catalytic region. Association of RLK5 with the KI domain is dependent on phosphorylation of RLK5 and can be abolished by dephosphorylation. KAPP may function as a signaling component in a pathway involving RLK5. ...
Previous data from our laboratory demonstrated significant protein phosphatase activity in the rat CL (Eyster et al. 1993, 1995, 1998). The phosphatase was identified as the PP2A based on its ability to preferentially dephosphorylate certain specific substrates over others and based on the activity of protein phosphatase inhibitors (Cohen 1991) against the luteal protein phosphatase activity (Eyster et al. 1993, 1995). The protein phosphatase activity in the corpora lutea of the pregnant rat decreased between days 10 and 12 of pregnancy; enzyme activity levels then remained low through day 20 of pregnancy (Eyster et al. 1998). These data led us to hypothesize that the decline in enzyme activity was due to a decrease in the expression of the catalytic subunits of PP2A, or to an increase in one of the B regulatory subunits of PP2A. This hypothesis was based on the heterotrimeric structure of the PP2A holoenzyme in which the B regulatory subunits inhibit enzyme activity of the catalytic subunits ...
Protein Phosphatase 1: 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.
Background: SNF1-related protein kinases 2 (SnRK2s) are key regulators of the plant response to osmotic stress. They are transiently activated in response to drought and salinity. Based on a phylogenetic analysis SnRK2s are divided into three groups. The classification correlates with their response to abscisic acid (ABA); group 1 consists SnRK2s non-activated in response to ABA, group 2, kinases non-activated or weakly activated (depending on the plant species) by ABA treatment, and group 3, ABA-activated kinases. The activity of all SnRK2s is regulated by phosphorylation. It is well established that clade A phosphoprotein phosphatases 2C (PP2Cs) are negative regulators of ABA-activated SnRK2s, whereas regulators of SnRK2s from group 1 remain unidentified. Results: Here, we show that ABI1, a PP2C clade A phosphatase, interacts with SnRK2.4, member of group 1 of the SnRK2 family, dephosphorylates Ser158, whose phosphorylation is needed for the kinase activity, and inhibits the kinase, both in ...
Reversible protein phosphorylation is widely accepted as a major mechanism for the control of biological processes in eukaryotic cells. In plants, reversible protein phosphorylation is involved in processes such as hormonal, pathogenic, or environmental stress responses (Mumby and Walter, 1993; Smith and Walker, 1993; Garbers et al., 1996; Schöntal, 1998;Janssens and Goris, 2001). In this context, Ser/Thr protein phosphatases (PPs) are important regulatory components of many signal transduction pathways (Ingebritsen and Cohen, 1983a; Schöntal, 1998). Several Ser/Thr phosphatases, grouped into different categories, have been identified in a variety of plant species. Specifically, homologs of the 1, 2A, and 2C types of animal PPs have been described in plants (Rodrı́guez, 1998; Lin et al., 1999; Meek et al., 1999). All these types of PPs are distinguished by their different sensitivity to inhibitors and their divalent cation requirements, and are structurally different (for review, see Mumby ...
By reversing the phosphorylation of key regulatory proteins mediated by protein kinases, phosphatases serve as an important complement to kinases and attenuate activated signal transduction pathways. Important classes of phosphatases include both receptor and nonreceptor protein tyrosine phosphatases (PTPs), dual specificity phosphatases (DUSPs), cell cycle regulatory phosphatases, the 4 major serine/threonine protein phosphatase gene families (PP1, PP2A, PP2B, and PP2C), and other increasingly important gene families (PP4, PP5, PP6, and PP7). PTPs regulate a variety of cellular processes including cell growth, differentiation, mitotic cycle, and oncogenic transformation. DUSPs can dephosphorylate serine and threonine as well as tyrosine residues, primarily targeting MAP kinases. PP1 family members regulate of a variety of cellular processes, such as cell division, glycogen metabolism, muscle contractility, protein synthesis, and HIV-1 viral transcription. PP2A family members negatively regulate ...
Type 1 serine/threonine protein phosphatase catalytic subunit; involved in various processes including glycogen metabolism, sporulation, mitosis; accumulates at mating projections by interaction with Afr1p; interacts with many regulatory subunits; involved in regulation of the nucleocytoplasmic shuttling of Hxk2p; import into nucleus is inhibited during spindle assembly checkpoint arrest ...
About one-third of all proteins in eukaryotic cells are usually phosphorylated at anybody time. various mobile processes was the main topic of an EMBO meeting that was arranged in De Panne Belgium (Sept 19-24 1999 by M.Bollen D.S and Barford.Klumpp. This Europhosphatase meeting attracted 170 individuals from 25 different countries. Book proteins phosphatase (regulators) Proteins phosphatases are categorized into three households predicated on the framework of their catalytic domains. The PPP family members BMS-509744 contains the phosphoserine/phosphothreonine-specific proteins phosphatases PP1 PP2A PP2B (calcineurin) PP4 and PP5. BMS-509744 The PPM family members comprises Mg2+-activated proteins phosphatases such as for example PP2C which also dephosphorylate phosphoserine and phosphothreonine residues. Protein-tyrosine phosphatases and dual-specificity proteins phosphatases which dephosphorylate all three phosphoamino acids participate in the PTP family members. S.Klumpp (Marburg Germany) ...
Protein Phosphatase Inhibitor-2 (I-2) specifically and instantaneously inhibits the catalytic subunit of type I protein phosphatase (PP1) at nanomolar concentrations. In contrast, the inhibition of native forms of PP1
Read Direct interactions of ABA-insensitive(ABI)-clade protein phosphatase(PP)2Cs with calcium-dependent protein kinases and ABA response element-binding bZIPs may contribute to turning off ABA response, Plant Molecular Biology on DeepDyve, the largest online rental service for scholarly research with thousands of academic publications available at your fingertips.
Background The malarial parasite, Plasmodium falciparum(Pf), is responsible for nearly 2 million deaths worldwide. However, the mechanisms of cellular signaling in the parasite remain largely...
title: 대장암 세포주에서 Fas 매개 세포 사멸(apoptosis)의 분자적 조절기전 : 세포사멸관련 유전자 발현 및 Protein Kinase C와 Protein Phosphatase의 역할, doi: none, category: Article
This gene encodes a serine/threonine phosphatase which is a member of the protein phosphatase catalytic subunit family. Proteins in this family participate in pathways regulated by reversible phosphorylation at serine and threonine residues; many of these pathways are involved in the regulation of cell growth and differentiation. The product of this gene has been shown to participate in signaling pathways in response to hormones or cellular stress, and elevated levels of this protein may be associated with breast cancer development. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Feb 2011 ...
Protein phosphatase involved in regulation of Akt and PKC signaling. Mediates dephosphorylation in the C-terminal domain hydrophobic motif of members of the AGC Ser/Thr protein kinase family; specifically acts on Ser-473 of AKT2 and AKT3, Ser-660 of PRKCB and Ser-657 of PRKCA (PubMed:15808505, PubMed:17386267, PubMed:18162466). Isoform 2 seems to have a major role in regulating Akt signaling in hippocampal neurons (By similarity). Akt regulates the balance between cell survival and apoptosis through a cascade that primarily alters the function of transcription factors that regulate pro- and antiapoptotic genes. Dephosphorylation of Ser-473 of Akt triggers apoptosis and suppression of tumor growth. Dephosphorylation of PRKCA and PRKCB leads to their destabilization and degradation (PubMed:18162466). Dephosphorylates STK4 on Thr-387 leading to STK4 activation and apoptosis (PubMed:20513427). Dephosphorylates RPS6KB1 and is involved in regulation of cap-dependent translation ...
To elucidate the roles of protein phosphatases type 1 (PP1) and type 2A (PP2A) in 1,25-dihydroxy-cholecalciferol [1,25(OH)2D3]-induced differentiation of HL-60 cells into monocytes, we examined the enzyme activity and the protein and gene expressions of PP1 and PP2A in these cells. Calyculin-A augmented the 1,25(OH)2D3-induced differentiation of the cells. Treatment of the cells with 1,25(OH)2D3 led to a decrease in PP1-like activity in the cytosol fraction, with a concomitant increase in the membrane and nuclear PP1-like activity, as determined when protein phosphatase activity was assayed using myosin light chain as substrate in the presence of 5 nm okadaic acid. Western blot analysis with antibodies specific for PP1 catalytic subunit isozymes (PP1α, PP1γ, and PP1δ) showed that all three PP1 isozymes were expressed but were differentially distributed in each cellular fraction. Subcellular redistribution of PP1-like activity during 1,25(OH)2D3-induced differentiation was mainly attributed to ...
Aromatase inhibitors (AIs) are effective endocrine therapeutics for postmenopausal women with estrogen receptor (ER)α‑positive breast cancer. However, the efficacy of the treatment is often limited by the onset of AI resistance, owing to the phosphorylation of ERα serine 167 (Ser167). Previous studies have indicated that hyperactivation of the phosphoinositide‑3 kinase/RAC serine/threonine‑protein kinase signaling pathway occurs in AI‑resistant breast cancer models, which coincides with elevated levels of ERα phosphorylation at Ser167. The tumor suppressor serine/threonine‑protein phosphatase 2A (PP2A) regulates the phosphatidylinositol 3‑kinase/RAC serine/threonine‑protein kinase signaling pathway. A previous study indicated that PP2A inhibition decreased ERα Ser167 phosphorylation and estradiol (E2)‑independent cell growth. The present study investigated the potential relevance of PP2A in E2 deprivation‑resistant MCF‑7 cells. E2 depletion reduced the susceptibility of ...
The degree of protein phosphorylation is regulated by a balance of protein kinase and phosphatase activities. Protein phosphatase-1 (PP1; see MIM 176875) is a signal-transducing phosphatase that influences neuronal activity, protein synthesis, metabolism, muscle contraction, and cell division. PPP1R14C is an inhibitor of PP1 (Liu et al., 2002 [PubMed 11812771]).[supplied by OMIM, Feb 2010 ...
Regulation of the major Ser/Thr phosphatase protein phosphatase 1 (PP1) is controlled by a diverse array of targeting and inhibitor proteins. Though many PP1 regulatory proteins share at least one PP1 binding motif, usually the RVxF motif, it was recently discovered that certain pairs of targeting a …
The present series of studies has analyzed two paradoxical observations on the action of H2O2 in neural plasticity: As seen previously (Gahtan et al., 1998), slices of Tg-SOD mice, which apparently overproduce H2O2, expressed lower LTP in response to the tetanic stimulation of afferent pathways than slices from normal mice. Surprisingly, this impairment could be overcome by the addition of H2O2 at a concentration that impaired LTP in the control wt mice. Conversely, aged tg-SOD mice exhibited larger LTP than that produced by wt slices. The effects of H2O2 were reversed in the aged mice; LTP in tg-SOD slices was impaired by the addition of H2O2, whereas LTP of wt slices was enhanced by H2O2.. In an attempt to resolve these paradoxical observations, we found that the young tg-SOD mice and the aged wt mice exhibited elevated levels of endogenous H2O2 and had different protein phosphatase activity with or without exogenous H2O2. Although protein phosphatases are considered to be facilitators of ...
3E7A: Crystal structures of protein phosphatase-1 bound to nodularin-R and tautomycin: a novel scaffold for structure-based drug design of serine/threonine phosphatase inhibitors
Protein phosphatase 5 (PP5) is a novel human protein serine/threonine phosphatase of molecular weight of 58 kDa. It is made up of a C-terminal…
A resource on protein phosphatases, a key class of regulatory proteins. Includes genomic and evolutionary analyses (phosphatomes), classification, disease associationa and an extensive database of protein phosphatase genes.
Unfair competition, in which a phosphatase and a phosphoprotein inhibitor/substrate mutually sequester each other from competing substrates and enzymes, is a conserved mechanism for the control of PPP family phosphatases.
Staphylococcus aureus; strain: USA300_FPR3757; locus tag: SAUSA300_1112 (SAUSA300_RS06020); symbol: stp1; product: protein phosphatase 2C domain-containing protein
15:30 But Ed didnt realize that the following year while my English didnt improve very much his deteriorated completely LOL. ...
SwePub titelinformation: Association of Protein Phosphatase PPM1G With Alcohol Use Disorder and Brain Activity During Behavioral Control in a Genome-Wide Methylation Analysis
A resource on protein phosphatases, a key class of regulatory proteins. Includes genomic and evolutionary analyses (phosphatomes), classification, disease associationa and an extensive database of protein phosphatase genes.
TY - JOUR. T1 - A ceramide-activated protein phosphatase mediates ceramide-induced G1 arrest of Saccharomyces cerevisiae. AU - Nickels, Joseph T.. AU - Broach, James R.. PY - 1996/2/15. Y1 - 1996/2/15. N2 - Certain mammalian growth modulators, such as tumor necrosis factor α, interleukin-1β, and γ-interferon, induce an antiproliferative response-terminal differentiation, apoptosisis, or cell cycle arrest-through a novel signal transduction pathway mediated by the lipid ceramide as a second messenger. Both a ceramide-activated protein phosphatase and a ceramide-activated protein kinase have been implicated in transmitting the signals elicited by ceramide. We have determined that ceramide addition to the yeast Saccharomyces causes a similar antiproliferative response, resulting in arrest of cells in the G1 phase of the cell cycle. We have also determined that yeast cells contain a ceramide-activated protein phosphatase composed of regulatory subunits encoded by TPD3 and CDC55 and a catalytic ...
p,Cantharidin is a natural toxin and an active constituent in a traditional Chinese medicine used to treat tumors. Cantharidin acts as a semi-selective inhibitor of PPP-family ser/thr protein phosphatases. Despite sharing a common catalytic mechanism and marked structural similarity with PP1C, PP2AC and PP5C, human PP4C was found to be insensitive to the inhibitory activity of cantharidin. To explore the molecular basis for this selectivity, we synthesized and tested novel C5/C6-derivatives designed from quantum-based modeling of the interactions revealed in the co-crystal structures of PP5C in complex with cantharidin. Structure-activity relationship studies and analysis of high-resolution (1.25Å) PP5C-inhibitor co-crystal structures reveal close contacts between the inhibitor bridgehead oxygen and both a catalytic metal ion and a non-catalytic phenylalanine residue, the latter of which is substituted by tryptophan in PP4C. Quantum chemistry calculations predicted that steric clashes with the ...
Supplementary Materialsijms-20-05994-s001. immune responses [15,16,17]. In addition, is usually up-regulated in the endometrial cells of pregnant women compared to non-pregnant women [18]. Up-regulated had been found in both the nucleus and cytoplasm in the decidual stromal cells of human first-trimester endometrium [18]. In an in vitro decidualization model, was up-regulated and only the short isoform translocated to the nucleus of endometrial stromal cells [18]. Given these facts, we were thinking about exploring the hyperlink between your macrophage and gene polarization in individual deciduas. Investigations of decidual macrophages polarity and stability may help to clarify their jobs in pregnancies and could pave the best way to therapies of pathological pregnancies. 2. Outcomes 2.1. NLRP7 Portrayed in Decidual Macrophages from the First-Trimester Being pregnant Our previous research discovered that may donate to the decidualization of endometrial stromal cells [18]. We continued to explore ...
Phosphodiesterase type 3B (PDE3B) has been shown to be activated and phosphorylated in response to insulin and hormones that increase cAMP. In order to study serine/threonine protein phosphatases involved in the regulation of rat adipocyte PDE3B, we investigated the phosphorylation and activation of PDE3B in vivoin response to phosphatase inhibitors and the dephosphorylation and deactivation of PDE3B in vitroby phosphatases purified from rat adipocyte homogenates. Okadaic acid and calyculin A induced dose- and time-dependent activation of PDE3B. Maximal effects were obtained after 30 min using 1 μM okadaic acid (1.8-fold activation) and 300 nM calyculin A (4-fold activation), respectively. Tautomycin and cyclosporin A did not induce activation of PDE3B. Incubation of adipocytes with 300 nM calyculin A inhibited protein phosphatase (PP) 1 and PP2A completely. Okadaic acid (1 μM) reduced PP2A activity by approx. 50% but did not affect PP1 activity, and 1 μM tautomycin reduced PP1 activity by ...
Apoptosis is important for tissue homeostasis and is the mechanism of cell death induced by many anticancer agents. The apoptotic machinery is present in all cells, such that tight regulation must exist to prevent untimely cell and tissue death. To avert apoptotic death, cells utilize survival signaling pathways including the PI3 kinase/Akt and MEK/ERK pathways. Inhibitors of serine/threonine protein phosphatases can inhibit drug-induced apoptosis, implicating these phosphatases in regulation of apoptotic pathways. Here, we determined which protein phosphatases (PP) are critical for this protection from apoptosis, and investigated the relationship between phosphatases and survival pathways. An apoptotic signal can be delivered through a receptor pathway or via drug-induced stress that triggers death via mitochondrial events. Chemical inhibitors of protein phosphatases, calyculin A, okadaic acid and tautomycin, prevented anisomycin-induced apoptosis, a model of the latter pathway. Concentrations ...
Apoptosis is important for tissue homeostasis and is the mechanism of cell death induced by many anticancer agents. The apoptotic machinery is present in all cells, such that tight regulation must exist to prevent untimely cell and tissue death. To avert apoptotic death, cells utilize survival signaling pathways including the PI3 kinase/Akt and MEK/ERK pathways. Inhibitors of serine/threonine protein phosphatases can inhibit drug-induced apoptosis, implicating these phosphatases in regulation of apoptotic pathways. Here, we determined which protein phosphatases (PP) are critical for this protection from apoptosis, and investigated the relationship between phosphatases and survival pathways. An apoptotic signal can be delivered through a receptor pathway or via drug-induced stress that triggers death via mitochondrial events. Chemical inhibitors of protein phosphatases, calyculin A, okadaic acid and tautomycin, prevented anisomycin-induced apoptosis, a model of the latter pathway. Concentrations ...
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Effect of serine/threonine protein kinases and protein phosphatases inhibitors on mitosis progression in a synchronized tobacco BY-2 culture ...
Buy our Recombinant Human Protein phosphatase 1 inhibitor subunit 2. Ab114835 is a full length protein produced in Wheat germ and has been validated in WB…
Influenza viruses of avian origin continue to pose pandemic threats to human health. Some of the H5N1 and H9N2 virus subtypes induce markedly elevated cytokine levels when compared with the seasonal H1N1 virus. We previously showed that H5N1/97 hyperinduces tumor necrosis factor (TNF)-alpha through p38 mitogen activated protein kinase (MAPK). However, the detailed mechanisms of p38MAPK activation and TNF-alpha hyperinduction following influenza virus infections are not known. Negative feedback regulations of cytokine expression play important roles in avoiding overwhelming production of proinflammatory cytokines. Here we hypothesize that protein phosphatases are involved in the regulation of cytokine expressions during influenza virus infection. We investigated the roles of protein phosphatases including MAPK phosphatase-1 (MKP-1) and protein phosphatase type 2A (PP2A) in modulating p38MAPK activation and downstream TNF-alpha expressions in primary human monocyte-derived macrophages (PBMac) infected
Shop Type-1 protein phosphatase inhibitor ELISA Kit, Recombinant Protein and Type-1 protein phosphatase inhibitor Antibody at MyBioSource. Custom ELISA Kit, Recombinant Protein and Antibody are available.
p,Protein phosphatases regulate mRNA synthesis and processing by remodeling the carboxy-terminal domain (CTD) of RNA polymerase II (Pol2) to dynamically inscribe a Pol2 CTD code. Fission yeast Fcp1 (SpFcp1) is an essential 723-amino acid CTD phosphatase that preferentially hydrolyzes Ser2-PO4 of the YS(2)PTSPS repeat. The SpFcp1 catalytic domain (aa 140-580) is composed of a DxDxT acyl-phosphatase module (FCPH) and a BRCT module. Here we conducted a genetic analysis of SpFcp1, which shows that (i) phosphatase catalytic activity is required for vegetative growth of fission yeast; (ii) the flanking amino-terminal domain (aa 1-139) and its putative metal-binding motif C(99)H(101)Cys(109)C(112) are essential; (iii) the carboxy-terminal domain (aa 581-723) is dispensable; (iv) a structurally disordered internal segment of the FCPH domain (aa 330-393) is dispensable; (v) lethal SpFcp1 mutations R271A and R299A are rescued by shortening the Pol2 CTD repeat array; and (vi) CTD Ser2-PO4 is not the only ...
The Arabidopsis thaliana type 1 protein phosphatase (PP1) catalytic subunit was released from its endogenous regulatory subunits by ethanol precipitation and purified by anion exchange and microcystin affinity chromatography. The enzyme was identified by MALDI-TOF mass spectrometry from a tryptic di …
Calcineurin (CaN) is a calcium and calmodulin dependent serine/threonine protein phosphatase (also known as protein phosphatase 3, and calcium-dependent serine-threonine phosphatase). It activates the T cells of the immune system and can be blocked by drugs. Calcineurin activates nuclear factor of activated T cell, cytoplasmic (NFATc), a transcription factor, by dephosphorylating it. The activated NFATc is then translocated into the nucleus, where it upregulates the expression of interleukin 2 (IL-2), which, in turn, stimulates the growth and differentiation of T cell response. Calcineurin is the target of a class of drugs called calcineurin inhibitors, which includes cyclosporin, voclosporin, pimecrolimus and tacrolimus. Calcineurin is a heterodimer of a 61-kD calmodulin-binding catalytic subunit, calcineurin A and a 19-kD Ca2+-binding regulatory subunit, calcineurin B. There are three isozymes of the catalytic subunit, each encoded by a separate gene (PPP3CA, PPP3CB, and PPP3CC) and two ...
The levels of the cytosolic serine/threonine protein phosphatases (PP) in rat adipocyte extracts have been determined, by using both reference substrates and hormone-sensitive lipase (HSL) as substrates. Adipocytes contain significant levels of both PP1 and 2A (1.6 and 2.0 m-units/ml of packed cells respectively), with lower levels of PP2C and virtually no PP2B activity. PP2A and 2C exhibit similar degrees of activity against HSL phosphorylated at site 1, together accounting for 92% of the total. In contrast, site 2 is dephosphorylated predominantly by PP2A (over 50% of total activity), whereas PP1 and PP2C contribute approx. 20% and 30% respectively to the total phosphatase activity against that site. Total phosphatase activity in the adipocyte extracts was 2-3-fold higher against site 2 than against site 1. The possible significance of these findings to the regulation of HSL activity in adipose tissue in vivo is discussed. ...
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Reversible protein phosphorylation catalyzed by protein kinases and phosphatases represents the most prolific and currently best-characterized post-translational modification. Over the last decade advancements in genome sequencing technologies has massively increased genomic databases, resulting in the identification of previously unannotated protein kinases and phosphatases from multiple organisms. The primary goal of the research presented here was to elucidate the evolutionary, biochemical, cellular and biological characteristics of two recently identified PPP-family protein phosphatase subclasses from the model photosynthetic Eukaryote Arabidopsis thaliana. These two subclasses included the Shewanella-like (SLP1 and 2) and Rhizobiales-like (RLPH2) phosphatases, which were named after their relatedness to phosphatase orthologs from Shewanella and Rhizobiales bacteria. Heterologous protein phosphatase expression in, and purification from, Escherichia coli revealed unique biochemical ...
Protein phosphatase 2A (PP2A) constitutes one of the major families of protein serine/threonine phosphatases found in all eukaryotic cells. PP2A holoenzymes are composed of a catalytic subunit complexed with a structural regulatory subunit of 65 kDa. These core subunits associate with regulatory subunits of various sizes to form different heterotrimers which have been purified and evaluated with regard to substrate specificity. In fully differentiated tissues PP2A expression levels are highest in the brain, however, relatively little is known about expression in the developing embryo. In order to determine the composition of PP2A catalytic subunits in the mouse, cDNAs were cloned and the genomic organization of PP2A Cα was determined. By a gene targeting approach in the mouse, we have previously shown that the absence of the major catalytic subunit of PP2A, Cα, resulted in embryonic lethality around embryonic day E6.5. No mesoderm was formed which implied that PP2A plays a crucial role in ...
The cyclic peptide hepatotoxins microcystin-LR, 7-desmethyl-microcystin-RR and nodularin are potent inhibitors of the protein phosphatases type 1 and type 2A. Their potency of inhibition resembles calyculin-A and to a lesser extent okadaic acid. These hepatotoxins increase the overall level of protein phosphorylation in hepatocytes. Evidence is presented to indicate that in hepatocytes the morphological changes and effects on the cytoskeleton are due to phosphatase inhibition. The potency of these compounds in inducing hepatocyte deformation is similar to their potency in inhibiting phosphatase activity. These results suggest that the hepatotoxicity of these peptides is related to inhibition of phosphatases, and further indicate the importance of the protein phosphorylation in maintenance of structural and homeostatic integrity in these cells. ...
article{972d3387-c0ca-4d23-9b0a-36720bbb1e75, abstract = {In adipocytes, protein kinase B (PKB) has been suggested to be the enzyme that phosphorylates phosphodiesterase 3B (PDE3B), a key enzyme in insulins antilipolytic signalling pathway. In order to screen for PKB phosphatases, adipocyte homogenates were fractionated using ion-exchange chromatography and analysed for PKB phosphatase activities. PKB phosphatase activity eluted as one main peak, which coeluted with serine/threonine phosphatases (PP)2A. In addition, adipocytes were incubated with inhibitors of PP. Incubation of adipocytes with 1 microM okadaic acid inhibited PP2A by 75% and PP1 activity by only 17%, while 1 microM tautomycin inhibited PP1 activity by 54% and PP2A by only 7%. Okadaic acid, but not tautomycin, induced the activation of both PKBalpha and PKBbeta. Finally, PP2A subunits were found in several subcellular compartments, including plasma membranes (PM) where the phosphorylation of PKB is thought to occur. In summary, ...
Phosphorylation and dephosphorylation events play an important role in the transmission of the ABA signal. Although SnRK2 [sucrose non-fermenting1-related kinase2] protein kinases and group A protein phosphatase type 2C (PP2C)-type phosphatases constitute the core ABA pathway, mitogen-activated protein kinase (MAPK) pathways are also involved in plant response to ABA. However, little is known about the interplay between MAPKs and PP2Cs or SnRK2 in the regulation of ABA pathways. In this study, an effort was made to elucidate the role of MAP kinase kinase kinase18 (MKKK18) in relation to ABA signaling and response. The MKKK18 knockout lines showed more vigorous root growth, decreased abaxial stomatal index and increased stomatal aperture under normal growth conditions, compared with the control wild-type Columbia line. In addition to transcriptional regulation of the MKKK18 promoter by ABA, we demonstrated using in vitro and in vivo kinase assays that the kinase activity of MKKK18 was regulated ...
Calyculin A is a serine/threonine phosphatase inhibitor that inhibits the activity of protein phosphatases PP1 and PP2A. Human carcinoma A431 cells treated with calyculin A for 30 minutes can undergo significant threonine phosphorylation, as shown by western blotting using anti-Phospho-Akt (Thr-34), cat.# AP1001, as co
The product of this gene belongs to the phosphatase 2A regulatory subunit B family. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell growth and division. It consists of a common heteromeric core enzyme, which is composed of a catalytic subunit and a constant regulatory subunit, that associates with a variety of regulatory subunits. The B regulatory subunit might modulate substrate selectivity and catalytic activity. This gene encodes a delta isoform of the regulatory subunit B56 subfamily. Alternatively spliced transcript variants encoding different isoforms have been identified. [provided by RefSeq, Jul 2008 ...
TY - JOUR. T1 - Characterization of the effect of TIMAP phosphorylation on its interaction with protein phosphatase 1. AU - Czikora, István. AU - Kim, Kyung Mi. AU - Kása, Anita. AU - Bécsi, Bálint. AU - Verin, Alexander D.. AU - Gergely, Pál. AU - Erdodi, Ferenc. AU - Csortos, Csilla. PY - 2011/7/1. Y1 - 2011/7/1. N2 - TIMAP, TGF-β inhibited, membrane-associated protein, is highly abundant in endothelial cells (EC). We have shown earlier the involvement of TIMAP in PKA-mediated ERM (ezrin-radixin-moesin) dephosphorylation as part of EC barrier protection by TIMAP (Csortos et al., 2008). Emerging data demonstrate the regulatory role of TIMAP on protein phosphatase 1 (PP1) activity. We provide here evidence for specific interaction (Ka = 1.80 × 10 6 M-1) between non-phosphorylated TIMAP and the catalytic subunit of PP1 (PP1c) by surface plasmon resonance based binding studies. Thiophosphorylation of TIMAP by PKA, or sequential thiophosphorylation by PKA and GSK3β slightly modifies the ...
TY - JOUR. T1 - Adiponectin-activated AMPK stimulates dephosphorylation of AKT through protein phosphatase 2A activation. AU - Kim, Kun Yong. AU - Baek, Ahmi. AU - Hwang, Ji Eun. AU - Choi, Yeon A.. AU - Jeong, Joon. AU - Lee, Myeong Sok. AU - Cho, Dea Ho. AU - Lim, Jong Seok. AU - Kim, Keun Il. AU - Yang, Young. PY - 2009/5/1. Y1 - 2009/5/1. N2 - Low serum levels of adiponectin are a high risk factor for various types of cancer. Although adiponectin inhibits proliferation and metastasis of breast cancer cells, the underlying molecular mechanisms remain obscure. In this study, we show that adiponectin-activated AMPK reduces the invasiveness of MDA-MB-231 cells by stimulating dephosphorylation of AKT by increasing protein phosphatase 2A (PP2A) activity. Among the various regulatory B56 subunits, B56& gammal was directly phosphorylated by AMPK at Ser 298 and Ser 336, leading to an increase of PP2A activity through dephosphorylation of PP2Ac at Tyr 307. We also show that both the blood levels of ...
Protein phosphatase 2A (PP2A) critically regulates cell signaling and is a human tumor suppressor. PP2A complexes are modulated by proteins such as cancerous inhibitor of protein phosphatase 2A (CIP2A), protein phosphatase methylesterase 1 (PME-1), and SET nuclear proto-oncogene (SET) that often are deregulated in cancers. However, how they impact cellular phosphorylation and how redundant they are in cellular regulation is poorly understood. Here, we conducted a systematic phosphoproteomics screen for phosphotargets modulated by siRNA-mediated depletion of CIP2A, PME-1, and SET (to reactivate PP2A) or the scaffolding A-subunit of PP2A (PPP2R1A) (to inhibit PP2A) in HeLa cells. We identified PP2A-modulated targets in diverse cellular pathways, including kinase signaling, cytoskeleton, RNA splicing, DNA repair, and nuclear lamina. The results indicate nonredundancy among CIP2A, PME-1, and SET in phosphotarget regulation. Notably, PP2A inhibition or reactivation affected largely distinct ...
Distinctive regulatory and metabolic properties of glycogen-targeting subunits of protein phosphatase-1 (PTG, GL, GM/RGl) expressed in hepatocytes.
Chattopadhyay D, Swingle MR, Salter EA, Wood E, DArcy B, Zivanov C, Abney K, Musiyenko A, Rusin SF, Kettenbach A, et al. Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C. Biochemical Pharmacology. 2016 ;109:14-26. ...
Chattopadhyay D, Swingle MR, Salter EA, Wood E, DArcy B, Zivanov C, Abney K, Musiyenko A, Rusin SF, Kettenbach A, et al. Crystal structures and mutagenesis of PPP-family ser/thr protein phosphatases elucidate the selectivity of cantharidin and novel norcantharidin-based inhibitors of PP5C. Biochemical Pharmacology. 2016 ;109:14-26. ...
TY - JOUR. T1 - Changes in the cytoskeleton of 3T3 fibroblasts induced by the phosphatase inhibitor, calyculin-A. AU - Hirano, Katsuya. AU - Chartier, Lynn. AU - Taylor, Richard G.. AU - Allen, Ronald E.. AU - Fusetani, Nobuhiro. AU - Karaki, Hideaki. AU - Hartshorne, David J.. PY - 1992/6. Y1 - 1992/6. N2 - Addition of the protein phosphatase inhibitor, calyculin-A, to 3T3 fibroblasts causes a marked change in cell morphology. Initially the cells become rounded, develop surface blebs and then detach from the substratum. In the detached cells an unusual ball-like structure is observed. This study focuses on the cytoskeleton during these calyculin-A-induced morphological changes. Stress fibres disappear as the cells begin to round and aggregates of actin are formed towards the apical surface of the cell. These aggregates condense, in the detached cells, to form the ball structure of approximately 3 μm diameter. Between the ball and the nucleus are cables of intermediate filaments that appear to ...
Reversible protein phosphorylation represents the cellular basis for integration of key signaling pathways, mediating a fine crosstalk between external effector molecules and intracellular events. In the heart, Ca2+ cycling and contractility are controlled by a fine balance of protein kinase and phosphatase activities in response to various second messenger signals. Demands on the hearts pumping action, during fight-or-flight situations, can increase human cardiac output by nearly 5-fold. This is linked to β-adrenergic activation of the cAMP dependent protein kinase (PKA). PKA then phosphorylates a set of key regulatory Ca2+ handling proteins that control excitation-contraction coupling cycle, such as phospholamban, the ryanodine receptor, the L-type Ca2+ channel, and troponin I.1. The protein kinases and their phosphoprotein substrates underlying augmentation of the hearts pumping action have been well characterized. However, similar studies on the protein phosphatases, reversing the ...
SWISS-MODEL Template Library (SMTL) entry for 3lc6.3. The alternative conformation structure of isocitrate dehydrogenase kinase/phosphatase from E. Coli
Protein phosphatase 1 (PP1; ∼38.5 kDa), a single-domain protein, is the most widely expressed and abundant serine/threonine phosphatase (1). By dephosphorylating a variety of protein substrates, PP1 regulates diverse biological processes, including protein synthesis, muscle contraction, carbohydrate metabolism, neuronal signaling and, of specific interest for this work, cell-cycle progression. Although the intrinsic substrate specificity of PP1 is very low, by interacting with regulatory proteins (∼200 biochemically confirmed PP1 interactors), PP1 achieves high specificity (2⇓⇓-5). The majority of PP1 regulators and some substrates bind PP1 via a primary PP1-binding motif, the RVxF motif, which binds to a hydrophobic groove on PP1 ∼20 Å distal from its catalytic center (6). Outside of the RVxF motif, PP1 regulatory proteins mostly lack any apparent sequence similarity. Thus, additional interaction sites, such as the SILK (7), the MyPhoNE (8), and the recently identified ΦΦ motif (9) ...
Protein Phosphatase 2A (PP2A) is a large family of enzymes that account for the majority of brain Ser/Thr phosphatase activity. While PP2A enzymes collectively modulate most cellular processes, sophisticated regulatory mechanisms are ultimately responsible for ensuring isoform-specific substrate specificity. Of particular interest to the Alzheimers disease (AD) field, alterations in PP2A regulators and PP2A catalytic activity, subunit expression, methylation and/or phosphorylation, have been reported in AD-affected brain regions.
TY - JOUR. T1 - Protein interactomes of protein phosphatase 2A B55 regulatory subunits reveal B55-mediated regulation of replication protein A under replication stress. AU - Wang, Feifei. AU - Zhu, Songli. AU - Fisher, Laura A.. AU - Wang, Weidong. AU - Oakley, Gregory G.. AU - Li, Chunling. AU - Peng, Aimin. PY - 2018/12/1. Y1 - 2018/12/1. N2 - The specific function of PP2A, a major serine/threonine phosphatase, is mediated by regulatory targeting subunits, such as members of the B55 family. Although implicated in cell division and other pathways, the specific substrates and functions of B55 targeting subunits are largely undefined. In this study we identified over 100 binding proteins of B55α and B55β in Xenopus egg extracts that are involved in metabolism, mitochondria function, molecular trafficking, cell division, cytoskeleton, DNA replication, DNA repair, and cell signaling. Among the B55α and B55β-associated proteins were numerous mitotic regulators, including many substrates of CDK1. ...
[ChEMBL Target Description] ID:CHEMBL3557, Name:Serine/threonine protein phosphatase 2A, 65 kDa regulatory subunit A, alpha isoform, Description:, Synonyms:
Protein phosphorylation plays roles in cell transformation. Numerous protein kinase enzymes actively participate in the formation of various types of cancer by phosphorylating downstream substrates. Aurora‑A is a widely known Serine/Threonine (Ser/Thr) oncogenic kinase, which is upregulated in more than twenty types of human cancer. This enzyme phosphorylates a wide range of substrates. For example, Aurora‑A induces cell transformation by phosphorylating hepatoma upregulated protein (HURP) at four serine residues, which in turn decreases the phosphorylated levels of cell‑growth suppressive Jun N‑terminal kinase (p‑JNK). Various protein phosphatase enzymes are considered tumor suppressors by the dephosphorylation and consequent inactivation of their oncogenic substrates. Protein phosphatase 1α (PP1α), for instance, acts on Aurora‑A by dephosphorylating its substrates. However, the role of PP1α in cancer progression remains ambiguous. PP1α is overexpressed in several cancer ...
Reversible protein phosphorylation is under the control of opposing activities of protein kinases and protein phosphatases, and has a crucial role in the regulation of cellular signal transduction in a plethora of neural cell functions, including neurogenesis, differentiation, gene transcription and cell death signalling (Klumpp & Krieglstein, 2002b). During the symposium, expert reviews of research on reversible protein phosphorylation, examples from screening approaches for kinase functions in neurons and studies on particular signalling pathways highlighted the importance of this fast‐emerging topic for the understanding of neuronal cell death, and the development of novel neuroprotective strategies.. Protein kinases have been established as key regulators in many important cellular processes, such as proliferation, maintenance of cell shape, survival signalling and apoptosis. Approximately 500 genes encode members of the kinase family in the human genome, and the predicted human kinome ...
The degradation of Ins(1,3,4,5)P4 in Dictyostelium was investigated using a mixture of [3H]Ins(1,3,4,5)P4 and [3-32P]Ins-(1,3,4,5)P4. After incubation of this mixture with a Dictyostelium homogenate the 32P/3H ratio found in the InsP3 product was reduced to 24% of the ratio in the substrate. 32P-labelled inorganic phosphate was found as well, whereas hardly any InsP2 was detected. This indicates that Ins(1,3,4,5)P4 is mainly degraded by a 3-phosphatase. The other enzyme was characterized by identification of the 32P-labelled InsP3 isomer. This isomer did not co-elute with Ins(1,3,4)P3, indicating that no 5-phosphatase was present in Dictyostelium. The 32P-labelled InsP3 could be oxidized using NaIO4. The only InsP3 isomer that has these characteristics is Ins(3,4,5)P3, indicating 1-phosphatase activity. The 1-phosphatase appeared to be dependent on MgCl2, whereas the 3-phosphatase was still active in the absence of MgCl2. An analogue of Ins(1,3,4,5)P4 with a thiophosphate substitution at the ...
Phosphoprotein levels are counterbalanced by phosphatases. Ultimately, transcriptional activation of certain target genes ...
Eto M, Karginov A, Brautigan DL (Jan 2000). "A novel phosphoprotein inhibitor of protein type-1 phosphatase holoenzymes". ... Protein phosphatase 1 regulatory subunit 14B is an enzyme that in humans is encoded by the PPP1R14B gene. GRCh38: Ensembl ... "Entrez Gene: PPP1R14B protein phosphatase 1, regulatory (inhibitor) subunit 14B". Dias Neto E, Correa RG, Verjovski-Almeida S, ... Tountas NA, Mandell JW, Everett AD, Brautigan DL (2005). "Juxtamembrane localization of the protein phosphatase-1 inhibitor ...
"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Molecular & Cellular Proteomics. 4 (11 ...
"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... Serine/threonine-protein phosphatase 4 regulatory subunit 3B is an enzyme that in humans is encoded by the SMEK2 gene. SMEK2 ... "A PP4-phosphatase complex dephosphorylates gamma-H2AX generated during DNA replication". Molecular Cell. 31 (1): 33-46. doi: ... evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity" (PDF). Molecular & Cellular Proteomics ...
"PP4R4/KIAA1622 Forms a Novel Stable Cytosolic Complex with Phosphoprotein Phosphatase 4". J. Biol. Chem. 283 (43): 29273-84. ... evolutionarily conserved protein phosphatase complex involved in cisplatin sensitivity". Mol. Cell. Proteomics. 4 (11): 1725-40 ...
"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... Serine/threonine-protein phosphatase 4 catalytic subunit is an enzyme that in humans is encoded by the PPP4C gene. PPP4C has ... Chen L, Dong W, Zou T, Ouyang L, He G, Liu Y, Qi Y (Aug 2008). "Protein phosphatase 4 negatively regulates LPS cascade by ... Hu MC, Tang-Oxley Q, Qiu WR, Wang YP, Mihindukulasuriya KA, Afshar R, Tan TH (Dec 1998). "Protein phosphatase X interacts with ...
1996). "Identification of the sites of interaction between lymphocyte phosphatase-associated phosphoprotein (LPAP) and CD45". J ... Protein tyrosine phosphatase receptor type C-associated protein is an enzyme that in humans is encoded by the PTPRCAP gene. The ... Vogel A, Strassburg CP, Manns MP (2003). "77 C/G mutation in the tyrosine phosphatase CD45 gene and autoimmune hepatitis: ... 1994). "LPAP, a novel 32-kDa phosphoprotein that interacts with CD45 in human lymphocytes". J. Biol. Chem. 269 (46): 29102-11. ...
Pandey AV, Mellon SH, Miller WL (2003). "Protein phosphatase 2A and phosphoprotein SET regulate androgen production by P450c17 ... 2007). "Lipid phosphate phosphatases 1 and 3 are localized in distinct lipid rafts". J. Biochem. 140 (5): 677-686. doi:10.1093/ ... 2003). "Protein phosphatase 2A (PP2A) regulates interleukin-4-mediated STAT6 signaling". J. Biol. Chem. 278 (5): 2787-2791. doi ... Lipid phosphate phosphohydrolase 1 also known as phosphatidic acid phosphatase 2a is an enzyme that in humans is encoded by the ...
This process is valuable in the extraction of proteins and specifically phosphoprotein and phosphopeptide phosphatases. Another ...
"The phosphorylation state of tau in the developing rat brain is regulated by phosphoprotein phosphatases". The Journal of ... Like kinases, phosphatases too play a role in regulating the phosphorylation of tau. For example, PP2A and PP2B are both ... Tau is a phosphoprotein with 79 potential Serine (Ser) and Threonine (Thr) phosphorylation sites on the longest tau isoform. ... Fujio K, Sato M, Uemura T, Sato T, Sato-Harada R, Harada A (July 2007). "14-3-3 proteins and protein phosphatases are not ...
... ion exchange chromatography was used to identify phosphoprotein phosphatase I and II. Since the discovery of these ... Tau dephosphorylation is catalysed by protein phosphatase-2A and phosphatase-2B. Deficiency or modification of one or both ... By using a desphosphorylating phosphatase, re-ligation can be avoided. These alkaline phosphatases are often sourced naturally ... and substrate specificities of phosphoprotein phosphatase(s) from rabbit liver". The Journal of Biological Chemistry. 251 (16 ...
"PP4R4/KIAA1622 forms a novel stable cytosolic complex with phosphoprotein phosphatase 4". The Journal of Biological Chemistry. ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... Chung H, Nairn AC, Murata K, Brautigan DL (Aug 1999). "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic ... Chung H, Nairn AC, Murata K, Brautigan DL (Aug 1999). "Mutation of Tyr307 and Leu309 in the protein phosphatase 2A catalytic ...
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... Wisniewski D, Strife A, Wojciechowicz D, Lambek C, Clarkson B (1994). "A 62-kilodalton tyrosine phosphoprotein constitutively ...
2000). "Phosphorylation of CPI-17, an inhibitory phosphoprotein of smooth muscle myosin phosphatase, by Rho-kinase". FEBS Lett ... Protein phosphatase 1 regulatory subunit 14A also known as CPI-17 (C-kinase potentiated Protein phosphatase-1 Inhibitor Mr = 17 ... There are three homologues of CPI-17: Phosphatase Holoenzyme Inhibitor (PHI: PPP1R14B), Kinase Enhanced Phosphatase Inhibitor ( ... an inhibitory phosphoprotein for myosin phosphatase". Biochem Biophys Res Commun. 285 (4): 1040-5. doi:10.1006/bbrc.2001.5290. ...
This latter enzyme is itself activated by protein kinase A and deactivated by phosphoprotein phosphatase-1. Protein kinase A ...
2000). "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl ... "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ...
Protein phosphatase 1 regulatory subunit 1B (PPP1R1B), also known as dopamine- and cAMP-regulated neuronal phosphoprotein ( ... "Entrez Gene: PPP1R1B protein phosphatase 1, regulatory (inhibitor) subunit 1B (dopamine and cAMP regulated phosphoprotein, ... monophosphate-regulated neuronal phosphoprotein. II. Comparison of the kinetics of phosphorylation of DARPP-32 and phosphatase ... This gene is also known as DARPP-32, highlighting its role as a dopamine- and cyclic AMP-regulated phosphoprotein. As such ...
In eukaryotic cells, phosphatases catalyze the removal of phosphate groups from tyrosine, serine and threonine phosphoproteins ... Tolstykh, T (2000). "Carboxyl methylation regulates phosphoprotein phosphatase 2A by controlling the association of regulatory ... The catalytic subunit of the major serine/threonine phosphatases, like Protein phosphatase 2 is covalently modified by the ... C-terminal protein methylation regulates the assembly of protein phosphatase. Methylation of the protein phosphatase 2A ...
As a phosphoprotein phosphatase, insulin dephosphorylates the enzyme, thus activating the PFK-2 and inhibiting the FBPase-2 ...
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... Src homology 2 (SH2) domain containing inositol polyphosphate 5-phosphatase 1 (SHIP1) is an enzyme with phosphatase activity. ... "The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ... "Association of tyrosine phosphatases SHP-1 and SHP-2, inositol 5-phosphatase SHIP with gp49B1, and chromosomal assignment of ...
"The phosphatidylinositol polyphosphate 5-phosphatase SHIP1 associates with the dok1 phosphoprotein in bcr-Abl transformed cells ...
Nakai C, Thomas JA (1974). "Properties of a phosphoprotein phosphatase from bovine heart with activity on glycogen synthase, ... Fluoride salts are commonly used in biological assay processing to inhibit the activity of phosphatases, such as serine/ ... Beryllium fluoride and aluminium fluoride are also used as phosphatase inhibitors, since these compounds are structural mimics ... 2008). "Crystal structures of a purple acid phosphatase, representing different steps of this enzyme's catalytic cycle". BMC ...
2001). "Phosphoprotein-protein interactions revealed by the crystal structure of kinase-associated phosphatase in complex with ... Gyuris J, Golemis E, Chertkov H, Brent R (Dec 1993). "Cdi1, a human G1 and S phase protein phosphatase that associates with ... The protein encoded by this gene belongs to the dual specificity protein phosphatase family. It was identified as a cyclin- ... Hannon, G J; Casso D; Beach D (Mar 1994). "KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases". ...
... is catalyzed by a phosphoprotein phosphatase called pyruvate dehydrogenase phosphatase. (Pyruvate dehydrogenase kinase should ...
For the SSH-1 protocol, see Secure Shell#Version 1.x Protein phosphatase Slingshot homolog 1 is an enzyme that in humans is ... 2004). "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. ... 2003). "Cell cycle-associated changes in Slingshot phosphatase activity and roles in cytokinesis in animal cells". J. Biol. ... 2004). "A pathway of neuregulin-induced activation of cofilin-phosphatase Slingshot and cofilin in lamellipodia". J. Cell Biol ...
Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell ... regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm". The ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit alpha isoform is an enzyme that in humans is encoded by the ...
"The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target ... Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... Serine/threonine-protein phosphatase 2A 56 kDa regulatory subunit beta isoform is an enzyme that in humans is encoded by the ...
"The B56 family of protein phosphatase 2A (PP2A) regulatory subunits encodes differentiation-induced phosphoproteins that target ... Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, and it is implicated in the negative control of cell ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... "Dephosphorylation of CDK9 by protein phosphatase 2A and protein phosphatase-1 in Tat-activated HIV-1 transcription". ...
This gene encodes the phosphatase 2A catalytic subunit. Protein phosphatase 2A is one of the four major Ser/Thr phosphatases, ... regulatory subunits encodes differentiation-induced phosphoproteins that target PP2A to both nucleus and cytoplasm". The ... "A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... Serine/threonine-protein phosphatase 2A catalytic subunit alpha isoform is an enzyme that (in humans) is encoded by the PPP2CA ...
PDPR: encoding protein Pyruvate dehydrogenase phosphatase regulatory subunit. *PKDTS: Polycystic kidney disease, infantile ... MPHOSPH6: encoding enzyme M-phase phosphoprotein 6. *MT1X: encoding protein Metallothionein 1X ...
phosphatase binding. • phosphoprotein phosphatase activity. • ion channel binding. • cytoskeletal protein binding. • protein C- ...
The reaction catalyzed by CDK is as follows: ATP + a target protein → {\displaystyle \rightarrow } ADP + a phosphoprotein. ... and acid/base phosphatase. Prior to the realization that individual enzymes were capable of such a task, it was believed that ...
Yu X, Chini CC, He M, Mer G, Chen J (October 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645 ... "Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha". Cancer Res. 62 (22): 6357-61. PMID ... Chen Y, Farmer AA, Chen CF, Jones DC, Chen PL, Lee WH (July 1996). "BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed ... BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases". Oncogene. 15 (2): 143-57. ...
phosphoprotein binding. • kinase binding. • protein binding. • androgen receptor binding. • identical protein binding. • enzyme ... "Direct interaction between the catalytic subunit of Protein Phosphatase 1 and pRb". Cancer Cell Int. 6: 3. doi:10.1186/1475- ...
Chen, Y; Farmer A A, Chen C F, Jones D C, Chen P L, Lee W H (1996). «BRCA1 is a 220-kDa nuclear phosphoprotein that is ... Regulation of BRCA1 phosphorylation by interaction with protein phosphatase 1alpha». Cancer Res. 62 (22): 6357-61. PMID ... Yu, Xiaochun; Chini Claudia Christiano Silva, He Miao, Mer Georges, Chen Junjie (2003). «The BRCT domain is a phospho-protein ... BRCA1b are tyrosine phosphoproteins that associate with E2F, cyclins and cyclin dependent kinases». Oncogene. 15 (2): 143-57. ...
... on amino acids, such as serine, threonine, and tyrosine results in the formation of a phosphoprotein, when the ... Barford D, Das AK, Egloff MP (1998). "The structure and mechanism of protein phosphatases: insights into catalysis and ... "Estimating the total number of phosphoproteins and phosphorylation sites in eukaryotic proteomes". GigaScience. 6: 1-11. doi: ... Kinases phosphorylate proteins and phosphatases dephosphorylate proteins. Many enzymes and receptors are switched "on" or "off ...
protein tyrosine phosphatase activity. • phosphatase activity. • phosphoprotein phosphatase activity. • hydrolase activity. • ... non-membrane spanning protein tyrosine phosphatase activity. • acid phosphatase activity. Cellular component. • cytoplasm. • ... It functions as an acid phosphatase and a protein tyrosine phosphatase by hydrolyzing protein tyrosine phosphate to protein ... ACP1, HAAP, LMW-PTP, acid phosphatase 1, soluble, LMWPTP, acid phosphatase 1. ...
An increase in blood sugar leads to secretion of insulin, which activates phosphoprotein phosphatase I, leading to ... "TIGAR TP53 induced glycolysis regulatory phosphatase [Homo sapiens (human)] - Gene - NCBI". www.ncbi.nlm.nih.gov. Retrieved ... It can behave as a phosphatase (Fructuose-2,6-Bisphosphatase) which cleaves the phosphate at carbon-2 producing F6P. It can ... and then converted to glucose by the liver-specific enzyme glucose 6-phosphatase and released into the blood. Glucagon and ...
phosphoprotein phosphatase activity. • phosphatidylinositol-3,4,5-trisphosphate 3-phosphatase activity. • phosphatidylinositol- ... Purple acid phosphatases - غلوكوز 6-فسفاتاز - Fructose bisphosphatase - Calcineurin - Phosphoprotein phosphatase (PP2A) - OCRL ... 3-phosphatase activity. • protein serine/threonine phosphatase activity. • protein tyrosine phosphatase activity. • protein ... PTEN, 10q23del, BZS, CWS1, DEC, GLM2, MHAM, MMAC1, 1, TEP1, phosphatase and tensin homolog, Phosphatase and tensin homolog, ...
de 1994). «KAP: a dual specificity phosphatase that interacts with cyclin-dependent kinases». Proc. Natl. Acad. Sci. U.S.A. ( ... de 1996). «BRCA1 is a 220-kDa nuclear phosphoprotein that is expressed and phosphorylated in a cell cycle-dependent manner». ... de 2000). «Dephosphorylation of human cyclin-dependent kinases by protein phosphatase type 2C alpha and beta 2 isoforms». J. ... de 2000). «NIPP1-mediated interaction of protein phosphatase-1 with CDC5L, a regulator of pre-mRNA splicing and mitotic entry ...
regulation of phosphoprotein phosphatase activity. • protein destabilization. • positive regulation of apoptotic process. • ...
negative regulation of phosphoprotein phosphatase activity. • liver development. • negative regulation of cyclic-nucleotide ... positive regulation of phosphatase activity. • GO:0032320, GO:0032321, GO:0032855, GO:0043089, GO:0032854 positive regulation ...
positive regulation of phosphoprotein phosphatase activity. • negative regulation of calcineurin-NFAT signaling cascade. • ... phosphoprotein binding. • RNA polymerase III type 2 promoter DNA binding. • protein kinase activity. • macromolecular complex ...
The receptor protein tyrosine phosphatase PTPmu (PTPRM) is capable of dephosphorylating PLCG1.[7] Two transcript variants ... and other phosphoproteins with Grb2 and the zeta-chain of the TCR". The Journal of Biological Chemistry. 270 (31): 18428-36. ... "Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration" ...
ADP + a phosphoprotein. Thus, the two substrates of this enzyme are ATP and a protein, whereas its two products are ADP and ... protein tyrosine phosphatase: Receptor-like protein tyrosine phosphatase. *Sh2 domain-containing protein tyrosine phosphatase ...
phosphatase activity. • phosphoprotein phosphatase activity. • hydrolase activity. • protein tyrosine phosphatase activity. ... Tyrosine-protein phosphatase non-receptor type 18 is an enzyme that in humans is encoded by the PTPN18 gene.[5][6] ... PTPN18, BDP1, PTP-HSCF, protein tyrosine phosphatase, non-receptor type 18. External IDs. MGI: 108410 HomoloGene: 74971 ... 2007). "A bioinformatics analysis of protein tyrosine phosphatases in humans". DNA Res. 12 (2): 79-89. doi:10.1093/dnares/12.2. ...
phosphoprotein binding. • protein binding. • MHC class II protein complex binding. • protein heterodimerization activity. • ... It interacts with CDC25 phosphatases, RAF1 and IRS1 proteins, suggesting its role in diverse biochemical activities related to ... "Specific interaction between 14-3-3 isoforms and the human CDC25B phosphatase". Oncogene. 19 (10): 1257-65. doi:10.1038/sj.onc. ... "14-3-3 proteins associate with cdc25 phosphatases". Proc. Natl. Acad. Sci. U.S.A. 92 (17): 7892-6. doi:10.1073/pnas.92.17.7892 ...
... (PSP)[1] is a form of phosphoprotein phosphatase that acts upon phosphorylated serine/ ... Shi Y (October 2009). "Serine/threonine phosphatases: mechanism through structure". Cell. 139 (3): 468-84. doi:10.1016/j.cell. ... Ser/Thr-specific protein phosphatases are regulated partly by their location within the cell and by specific inhibitor proteins ... Serine and threonine phosphates are stable under physiological conditions, so a phosphatase enzyme has to remove the phosphate ...
PTPLAD1: encoding enzyme Protein tyrosine phosphatase-like protein PTPLAD1. *PYGO1: encoding protein Pygopus homolog 1 ( ... ARPP-19: encoding protein cAMP-regulated phosphoprotein 19. *C15orf15: encoding protein Probable ribosome biogenesis protein ...
Holsinger LJ, Ward K, Duffield B, Zachwieja J, Jallal B (2002). "The transmembrane receptor protein tyrosine phosphatase DEP1 ... "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. doi: ... "The receptor-like protein-tyrosine phosphatase DEP-1 is constitutively associated with a 64-kDa protein serine/threonine kinase ...
The encoded protein is a tyrosine phosphatase and belongs to the Cdc25 phosphatase family. It directs dephosphorylation of ... "The essential mitotic peptidyl-prolyl isomerase Pin1 binds and regulates mitosis-specific phosphoproteins". Genes Dev. UNITED ... M-phase inducer phosphatase 3 is an enzyme that in humans is encoded by the CDC25C gene. This gene is highly conserved during ... Nilsson I, Hoffmann I (2000). "Cell cycle regulation by the Cdc25 phosphatase family". Progress in Cell Cycle Research. 4: 107- ...
... protein-tyrosine-phosphatase - proteinoid - proteomics - protirelin - proto-oncogene - proto-oncogene proteins - proto-oncogene ... phosphoprotein - phosphorus - phosphorylation - phosphoserine - phosphothreonine - phosphotyrosine - photobiology - photolysis ...
Ishino M, Ohba T, Sasaki H, Sasaki T (1995). "Molecular cloning of a cDNA encoding a phosphoprotein, Efs, which contains a Src ... Liu F, Hill DE, Chernoff J (1996). "Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src ... Bradbury P, Mahmassani M, Zhong J, Turner K, Paul A, Verrills NM, O'Neill GM (2012). "PP2A phosphatase suppresses function of ... a novel mechanism of protein tyrosine phosphatase substrate recognition". Oncogene. 15 (8): 877-85. doi:10.1038/sj.onc.1201279 ...
"A PP2A phosphatase high density interaction network identifies a novel striatin-interacting phosphatase and kinase complex ... "Large-scale characterization of HeLa cell nuclear phosphoproteins". Proc. Natl. Acad. Sci. U.S.A. 101 (33): 12130-5. doi: ... "A mammalian homolog of yeast MOB1 is both a member and a putative substrate of striatin family-protein phosphatase 2A complexes ... nuclear autoantigen are members of a novel family of calmodulin-binding proteins that associate with protein phosphatase 2A". J ...
... It is incumbent on most of us while experts in neuro-scientific ... Subsequently, a lot more than 4 million toddlers are already https://en.wikipedia.org/wiki/Phosphoprotein_phosphatase brought ...
PP: Phosphoprotein phosphatase. PP1: Phosphoprotein phosphatase 1. PP2A: Phosphoprotein phosphatase 2A. PP2B: Phosphoprotein ... PP2C: Phosphoprotein phosphatase 2C. PPM: Phosphoprotein phosphatase M family. PPP: Phosphoprotein phosphatase P family. RIPP: ... Pereira, SR., et al., The phosphoprotein phosphatase family of Ser/Thr phosphatases as principal targets of naturally occurring ... phosphatase 2A (PP2A) does not require such cations, whereas phosphatase 2B (PP2B, also known as calcineurin) and phosphatase ...
... Chandrama Shrestha,1 ... Chandrama Shrestha, Yuanyuan Tang, Hong Fan, et al., "Phosphoprotein Phosphatase 1 Is Required for Extracellular Calcium- ...
We concluded that the 18-22 PPP genes of Drosophilidae were generated from a core set of 8 indispensable phosphatases that are ... During the course of these studies we identified 5, up till now uncharacterized phosphatase retrogenes: PpY+, PpD5+, PpD6+, ... Retropositons followed by tandem gene duplications extended the phosphatase repertoire, and sporadic gene losses contributed to ... Phosphoprotein phosphatases (PPP), these ancient and important regulatory enzymes are present in all eukaryotic organisms. ...
A High-throughput Assay for Phosphoprotein-specific Phosphatase Activity in Cellular Extracts. Anjun K. Bose and Kevin A. Janes ... Phosphatase activity is determined by the drop in phosphoprotein signal in lysate-treated samples relative to negative controls ... A high-throughput phosphatase assay that monitors endogenous activity toward specific phosphoprotein substrates. A, recombinant ... 1988) Protein phosphatase-1 and protein phosphatase-2A from rabbit skeletal muscle. Methods Enzymol. 159, 390-408. ...
phosphoprotein phosphatase can also refer to... phosphoprotein phosphatase Effects of sulfhydryl regents on the activity of ... Rrd1p, an RNA polymerase II-specific prolyl isomerase and activator of phosphoprotein phosphatase, promotes transcription ... complex in Jurkat T cells lacking expression of lymphocyte phosphatase-associated phosphoprotein. ... EC 3.1.3.16; systematic name: phosphoprotein phosphohydrolase; any enzyme that removes a phosphate group from a protein by ...
Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for ... Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for ... Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for ... Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for ...
... dopamine and cAMP regulated phosphoprotein, DARPP-32)), Authors: Wael El-Rifai, Abbes Belkhiri. Published in: Atlas Genet ... PPP1R1B (protein phosphatase 1, regulatory (inhibitor) subunit 1B (dopamine and cAMP regulated phosphoprotein, DARPP-32)). ... PPP1R1B (protein phosphatase 1, regulatory (inhibitor) subunit 1B (dopamine, cAMP regulated phosphoprotein, DARPP-32)). ... DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1.. ...
... dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in ... PPP1R1B; protein phosphatase 1, regulatory (inhibitor) subunit 1B (dopamine and cAMP regulated phosphoprotein, DARPP-32); DARPP ... protein phosphatase 1, regulatory (inhibitor) subunit 1B (dopamine and cAMP regulated phosphoprotein, DARPP-32). ... DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly ...
... from the phosphoprotein phosphatase (PPP) family. Conclusions: Phosphatase ABI1 and okadaic acid-sensitive phosphatases of the ... Phosphatase ABI1 and okadaic acid-sensitive phosphoprotein phosphatases inhibit salt stress-activated SnRK2.4 kinase. Mostrar ... Phosphatase ABI1 and okadaic acid-sensitive phosphoprotein phosphatases inhibit salt stress-activated SnRK2.4 kinase. RiuNet: ... Phosphatase ABI1 and okadaic acid-sensitive phosphoprotein phosphatases inhibit salt stress-activated SnRK2.4 kinase ...
... derived by this method were approximately 30,500 for phosphoprotein phosphatase I and 34,000 for phosphoprotein phosphatase II ... The phosphoprotein phosphatase(s) acting on muscle phosphorylase a was purified from rabbit liver by acid precipitation, high ... Enzyme activity was recovered in the final step as two distinct peaks tentatively referred to as phosphoprotein phosphatases I ... Purification and properties of a heat-stable protein inhibitor of phosphoprotein phosphatase from rabbit liver. (opens in new ...
Protein phosphorylation by kinases with its converse dephosphorylation by phosphatases regulates most biological processes. In ... Nasa, Isha; Kettenbach, Arminja N (2018) Coordination of Protein Kinase and Phosphoprotein Phosphatase Activities in Mitosis. ... Mechanisms of phosphorylation signaling by phosphoprotein phosphatases Kettenbach, Arminja Nadine Dartmouth College, Hanover, ... Mechanisms of phosphorylation signaling by phosphoprotein phosphatases. Kettenbach, Arminja Nadine / Dartmouth College. ...
Lung cancer; Oncology; Phosphoprotein phosphatases; Therapeutics; Tumor suppressors. PMID:. 30830869. PMCID:. PMC6478418. DOI: ... The tumor suppressor protein phosphatase 2A (PP2A) acts as a negative regulator of these pathways. We hypothesize that ...
phosphoprotein phosphatase activity IBA Inferred from Biological aspect of Ancestor. more info ... Title: Phosphatase activity of small C-terminal domain phosphatase 1 (SCP1) controls the stability of the key neuronal ... CTDSP1 CTD small phosphatase 1 [Homo sapiens] CTDSP1 CTD small phosphatase 1 [Homo sapiens]. Gene ID:58190 ... This gene encodes a member of the small C-terminal domain phosphatase (SCP) family of nuclear phosphatases. These proteins play ...
Phosphoprotein Phosphatases / genetics * Phosphoprotein Phosphatases / metabolism* * Restriction Mapping * Second Messenger ... Multiple protein-aspartate phosphatases provide a mechanism for the integration of diverse signals in the control of ... These phosphatases function to drain the phosphorelay, lower Spo0A approximately P levels, and prevent sporulation. The ... We describe here a family of protein-aspartate phosphatases with activity on Spo0F approximately P, a response regulator ...
... enzymes constitute a large family of Ser/Thr phosphatases with multiple functions in cellular signaling and physiology. The ... Phosphoprotein Phosphatases / metabolism* * Protein O-Methyltransferase / metabolism * Protein Phosphatase 2 / biosynthesis * ... Protein phosphatase type 2A (PP2A) enzymes constitute a large family of Ser/Thr phosphatases with multiple functions in ... The biogenesis of active protein phosphatase 2A holoenzymes: a tightly regulated process creating phosphatase specificity FEBS ...
GO:0004721 phosphoprotein phosphatase activity Cellular Component. No terms assigned in this category. ... Kinase associated protein phosphatase (IPR016660). Short name: Kinase_assoc_Pase Family relationships *Protein phosphatase 2C ... The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase ... This entry represents a group of kinase associated protein phosphatases from plants, including KAPP (also known as protein ...
Phosphoprotein phosphatase PPZ/Ppq1 (IPR011159). *Sphingomyelin phosphodiesterase (IPR011160). *Serine/threonine protein ... Serine/threonine-protein phosphatase PP1 catalytic subunit alpha/beta (IPR037979). *Serine/threonine-protein phosphatase PP1- ... Metallo-dependent phosphatase-like (IPR029052). Short name: Metallo-depent_PP-like Overlapping entries *Phosphodiesterase ... Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a mu-(hydr)oxo bridged di-iron ...
Phosphoprotein. Proteomic databases. Encyclopedia of Proteome Dynamics. More...EPDi. Q9QZ67. MaxQB - The MaxQuant DataBase ... Protein phosphatase 1DAdd BLAST. 598. Amino acid modifications. Feature key. Position(s). DescriptionActions. Graphical view. ... PPM-type phosphatasePROSITE-ProRule annotation. ,p>Manual validated information which has been generated by the UniProtKB ... Protein phosphatase 1D (EC:3.1.3.16*Search proteins in UniProtKB for this EC number. ...
... calmodulin-stimulated protein phosphatase which plays an essential role in the transduction of intracellular Ca(2+)-mediated ... Phosphoprotein. Proteomic databases. Encyclopedia of Proteome Dynamics. More...EPDi. P48454. jPOST - Japan Proteome Standard ... Serine/threonine-protein phosphatase 2B catalytic subunit gamma isoform (EC:3.1.3.16*Search proteins in UniProtKB for this EC ... calmodulin-dependent protein phosphatase activity Source: UniProtKB ,p>Inferred from Direct Assay,/p> ,p>Used to indicate a ...
Phosphoprotein phosphatase 2A MTases 166. VP39 An mRNA CapSpecific 255. Interaction between VP39s two functions ...
Preserve the integrity of phosphoproteins in your samples. Phosphatase inhibitor cocktails and tablets contain chemical ... Thermo Scientific Pierce Phosphatase Inhibitors preserve protein phosphorylation from phosphatases in cell and tissue extracts. ... acid and alkaline phosphatase activity was determined in mouse brain extract following treatment with Pierce Phosphatase ... Preserve protein phosphorylation from phosphatases in cell and tissue extracts #cq-image-jsp-bcf641f9-4057-4c8a-9ed5- ...
Phosphoprotein phosphatase. Category. › Molecular function. Gene Ontology. More...GOi. › phosphoprotein phosphatase activity [ ... While many protein phosphatases inhibit the activities of phosphorylation cascades, some activate them. ...
Activates phosphoprotein phosphatase. GLUCAGON/INSULIN RATIO IN BLOOD (see appendix). Increases when gluconeogenesis is needed ... Enzyme: Glucose 6-phosphatase. Note: This is not a reversal of PFK-1 reaction; ATP is not. produced when phosphate group is ... Glucose 6-Phosphatase. Glucose 6 phosphate Glucose. Induced during fasting. In luminal side of the ER. Present in liver and ... glucose-6-phosphatase. Skeletal muscles do not. convert glucose-6-phosphate glucose due to the. absence of the enzyme. Control ...
Phosphoprotein phosphatase. TIP41:. TIP41-like family protein. TUB:. Beta-tubulin. UBQ:. Ubiquitin. ...
Phosphoprotein. phosphatase. Insulin. (high glucose, after glycogen stores are maxed,has already made pyruvate and citrate). ( ... 6-Phosphatase. MALATE. SHUTTLE. (3-Hydroxy-3-methylglutaryl CoA). (Fed state). (Fasting state). (Fasting state). (Fed state). ( ... Phosphatase. Insulin. Protein. Kinase A. Protein. Kinase A. Palmitate (16C). 14 NADPH. 14 NADP+. Chain elongaton. (adding ...
Phosphoprotein Phosphatases, Phosphoproteins, Protein Phosphatase 1. Abstract. The neurotransmitter dopamine has been ... Thus, the basal ganglia of mammalian brain contain a region-specific neuronal phosphoprotein that is a protein phosphatase ... DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1.. ... DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1.. ...
protein phosphatase-2A;. DARPP-32,. dopamine- and cAMP-regulated phosphoprotein of 32 kDa;. Cdk5,. cyclin-dependent kinase 5;. ... Protein kinase A activates protein phosphatase 2A by phosphorylation of the B56δ subunit. Jung-Hyuck Ahn, Thomas McAvoy, Sergey ... In the current study, we have elucidated a mechanism whereby protein phosphatase 2A (PP2A) is activated by a cAMP/PKA-dependent ... Our studies focused on the dephosphorylation of DARPP-32 by B56δ/PP2A but this heterotrimeric form of the phosphatase is likely ...
1991) Protein phosphatases: recent progress. Adv Second Messenger Phosphoprotein Res 23:1-121. ... The protein phosphatase 1 and 2A inhibitors prevent the LFS-induced depotentiation. A,C, Example of an experiment showing that ... Fourth, protein phosphatase 1 and 2A inhibitors okadaic acid and calyculin A greatly reduced the depotentiation produced by LFS ... 1989) Calyculin A and okadaic acid: inhibitors of protein phosphatase activity. Biochem Biophys Res Commun 159:871-877. ...
... phosphoprotein and phosphopeptide quantitation assays. Power your research with Pro-Q® Diamond technology, and get results ... These kits are ideal for measuring phosphatase and kinase activity and for monitoring relative phosphoprotein or phosphopeptide ... Detect phosphoproteins on microarrays The Pro-Q Diamond phosphoprotein/phosphopeptide microarray stain directly detects ... Detect phosphoproteins in polyacrylamide gels and blots Pro-Q Diamond phosphoprotein stains are ideal for analysis of ...
  • Genes coding for phosphoserine/threonine phosphatases are less numerous in vertebrate genomes than those for serine /threonine kinases, and the complexity of phosphatases function arises in part from the interactions of catalytic subunits with other proteins. (sigmaaldrich.com)
  • Molecular cloning revealed that serine/threonine phosphatases belong to two different families of about a dozen of genes each in mammals: the phosphoprotein phosphatase P (PPP) family includes PP1, PP2A, PP2B, and a few related enzymes, PP4, PP5, PP6 and PP7, while the phosphoprotein phosphatase M family (PPM) includes PP2C and related enzymes. (sigmaaldrich.com)
  • The serine/threonine phosphatases of the PPP family are mostly regulated by protein-protein interactions. (sigmaaldrich.com)
  • Phosphatase inhibitor cocktails and tablets contain chemical compounds that target serine, threonine, and tyrosine phosphatases. (thermofisher.com)
  • Phosphorylation at Thr-34 converts DARPP-32 into a potent, high-affinity inhibitor of the broad specificity serine/threonine protein phosphatase, PP-1, leading to increased phosphorylation of many physiologically important substrates in medium spiny neurons, including neurotransmitter receptors, voltage-gated ion channels, ion pumps, protein kinases, and transcription factors ( 1 , 2 ). (pnas.org)
  • Protein phosphatase 2A (PP2A) refers to a ubiquitous, highly conserved family of at least 96 serine/threonine phosphatases that represent 0.1-1% of total cellular proteins and play a crucial role in regulating most cellular functions (Reviewed in Virshup and Shenolikar, 2009 ). (frontiersin.org)
  • Here, we identify PP1 as a serine/threonine phosphatase that associates with and dephosphorylates AKT in breast cancer cells, and we show that ErbB2 inhibits PP1-dependent dephosphorylation of AKT. (aacrjournals.org)
  • Protein phosphatase 1 (PP1) belongs to a certain class of phosphatases known as protein serine/threonine phosphatases. (wikipedia.org)
  • The cocktail is provided as a ready-to-use broad-spectrum solution of inhibitors targeting both serine/threonine phosphatases and protein tyrosine phosphatases (PTPs). (activemotif.com)
  • The Phosphatase Inhibitor Cocktail is a broad-spectrum solution of phosphatase inhibitors specific for serine/threonine as well as protein tyrosine phosphatases (PTPs). (activemotif.com)
  • In eukaryotes, dephosphorylation on serine/threonine residues is effected by two distinct groups of functionally diverse phosphatases, the phosphoprotein M (represented by a sole member in higher eukaryotes, PP2C) and PPP 1 families ( 1 ). (mcponline.org)
  • The large number of PPP1Rs reflects the wide substrate range of the serine/threonine phosphatase holoenzymes. (genenames.org)
  • Protein Ser/Thr phosphatases are a group of enzymes that catalyze the removal of phosphate groups from serine and/or threonine residues by hydrolysis of phosphoric acid monoesters. (genecards.org)
  • ARPP-16 Is a Striatal-Enriched Inhibitor of Protein Phosphatase 2A Regulated by Microtubule-Associated Serine/Threonine Kinase 3 (Mast 3 Kinase). (yale.edu)
  • Beyond the dopamine receptor: regulation and roles of serine/threonine protein phosphatases. (yale.edu)
  • A eukayrotic protein serine-threonine phosphatase subtype that dephosphorylates a wide variety of cellular proteins. (curehunter.com)
  • Classification of protein serine/threonine phosphatases: Identification and quantitation in cell extracts. (currentprotocols.com)
  • Protein serine/threonine phosphatases: New avenues for cell regulation. (currentprotocols.com)
  • Protein (serine, threonine) phosphate phosphatases. (currentprotocols.com)
  • Protein phosphatase 1 (PP1) is a major eukaryotic protein serine/threonine phosphatase that regulates an enormous variety of cellular functions through the interaction of its catalytic subunit (PP1c) with over fifty different established or putative regulatory subunits. (biologists.org)
  • however, comprise only ∼150 members, of which fewer than 40 are serine/threonine phosphatases (International human genome sequencing consortium). (biologists.org)
  • Type 1 protein phosphatases (PP1) dephosphorylate the β-subunit of phosphorylase kinase and are inhibited by phospho-inhibitor-1 and inhibitor-2, whereas type 2 protein phosphatases (PP2) dephosphorylate the α-subunit of phosphorylase kinase and are resistant to the aforementioned inhibitors. (sigmaaldrich.com)
  • Regulatory subunit (CNB1 gene product) of yeast Ca2+/calmodulin-dependent phosphoprotein phosphatases is required for adaptation to pheromone. (asm.org)
  • The composition of heterotrimeric PP2A holoenzymes, resulting from the combinatorial assembly of a catalytic C subunit, a structural A subunit, and regulatory B-type subunit, provides the essential determinants for substrate specificity, subcellular targeting, and fine-tuning of phosphatase activity, largely explaining why PP2A is functionally involved in so many diverse physiological processes, sometimes in seemingly opposing ways. (nih.gov)
  • We have found that the A/C subunits of PP2A, in association with the B56δ (or PPP2R5D) regulatory subunit, is an active DARPP-32 phosphatase. (pnas.org)
  • This gene encodes the phosphatase 2A catalytic subunit. (genecards.org)
  • PPP2CB (Protein Phosphatase 2 Catalytic Subunit Beta) is a Protein Coding gene. (genecards.org)
  • PPP3CC (Protein Phosphatase 3 Catalytic Subunit Gamma) is a Protein Coding gene. (genecards.org)
  • Several isoforms of the protein phosphatase catalytic subunit exist due to the presence of multiple genes and the alternative splicing of their mRNAs. (curehunter.com)
  • Phosphoprotein phosphatases, which hydrolyze the phosphoester bonds of phosphoserines, phosphothreonines or phosphotyrosines, play an essential role in signal transduction and actively contribute to the regulation of protein phosphorylation. (sigmaaldrich.com)
  • Once thought of as global attenuators of phosphorylation ( 2 ), PPases are now known to recognize specific subsets of phosphoprotein targets ( 4 ⇓ ⇓ - 7 ). (mcponline.org)
  • Activation of PKA or PKG leads to phosphorylation of DARPP-32 at Thr34 and subsequently converts DARPP-32 into a potent inhibitor of protein phosphatase-1 (PP-1). (atlasgeneticsoncology.org)
  • Results: Here, we show that ABI1, a PP2C clade A phosphatase, interacts with SnRK2.4, member of group 1 of the SnRK2 family, dephosphorylates Ser158, whose phosphorylation is needed for the kinase activity, and inhibits the kinase, both in vitro and in vivo. (upv.es)
  • Protein phosphorylation by kinases with its converse dephosphorylation by phosphatases regulates most biological processes. (grantome.com)
  • The occupancy of a given phosphorylation site reflects the balance between the activities of kinases and phosphatases. (grantome.com)
  • To understand the reversible nature of protein phosphorylation, we must investigate the forward and reverse reaction by connecting kinases and phosphatases on their shared substrates of interest. (grantome.com)
  • Protein phosphorylation is catalyzed by more than 500 protein kinases, however, most protein dephosphorylation is carried out by only seven phosphoprotein phosphatases (PPPs). (grantome.com)
  • We envision this work to be a resource for the phosphorylation signaling community, as well as a framework for future research into phosphatase biology. (grantome.com)
  • While many protein phosphatases inhibit the activities of phosphorylation cascades, some activate them. (uniprot.org)
  • The state of phosphorylation of DARPP-32 can be regulated by dopamine and by cyclic AMP in intact nerve cells, suggesting a role for this phosphoprotein in mediating certain of the effects of dopamine on dopaminoceptive cells. (cornell.edu)
  • Pro-Q Diamond phosphoprotein stains are ideal for analysis of phosphorylation of a single protein or an entire proteome. (thermofisher.com)
  • The level of myosin II phosphorylation is determined by activities of myosin light chain kinase and myosin phosphatase (MP). (biomedsearch.com)
  • These data indicate that ErbB2 acts to preserve the phosphorylation, and hence to prolong the activation, of AKT kinase by repressing the activity of the phosphatase PP1. (aacrjournals.org)
  • One mechanism, which appears not to depend on the phosphatase activity of SHP-2, is through tyrosine phosphorylation of SHP-2 as observed in response to PDGF, IL-3, and IL-6-type cytokines ( 19 , 45 , 77 ). (asm.org)
  • Among the possible tyrosine phosphorylation sites that reside primarily in the C-terminal half of SHP-2, which also harbors the phosphatase domain, are four sites with the YXNX motifs known to serve as docking element for Grb2 (growth factor receptor binding protein 2). (asm.org)
  • n = 10) for the following parameters: βAR density, G-coupled receptor kinases 2 and 5, stimulatory and inhibitory G-proteins, phosphorylation of myofilament targets of PKA, protein phosphatase 1, phospholamban, SERCA2a and single myocyte contractility. (curehunter.com)
  • Not all phosphorylation sites are accessible for dephosphorlyation by AP (due to steric hindrances), and other phosphatases (e.g., specific phosphoprotein phosphatases or acidic phosphatases) may have to be used. (sigmaaldrich.com)
  • The various sites of protein phosphorylation are described along with the roles of the many kinases and phosphatases that regulate phosphorylation. (currentprotocols.com)
  • How do such a small number of protein phosphatases dephosphorylate thousands of proteins while allowing the level of phosphorylation of each of these proteins to be regulated independently? (biologists.org)
  • Protein kinases, together with their cognate phosphatases, play a central role in signal transduction by catalyzing reversible protein phosphorylation. (asm.org)
  • Protein phosphorylation, which plays a key role in most cellular activities, is a reversible process mediated by protein kinases and phosphoprotein phosphatases. (embl-heidelberg.de)
  • In this section of the gel, the computer-generated overlay of the two staining patterns reveals the phosphoproteins (magenta), and nonphosphorylated proteins (green). (thermofisher.com)
  • The Pro-Q Diamond phosphoprotein/phosphopeptide microarray stain directly detects phosphorylated proteins or peptides on microarrays-no antibodies or radioisotopes are required. (thermofisher.com)
  • The latter makes these amino acid sequences crossroads for signaling and motif strength between kinases, pSer/pThr-binding proteins and phosphatases. (portlandpress.com)
  • It is recommended to use 10 µl of the Phosphatase Inhibitor Cocktail solution to inhibit dephosphorylation of proteins for 1 ml of lysate. (activemotif.com)
  • and 9 ), but whether these proteins represent bona fide regulatory subunits or phosphatase substrates and how these binding proteins may affect PP4 activity are unclear. (mcponline.org)
  • PPP1R subunits (also known as PP1-interacting proteins, or PIPs) direct the substrate specificity of protein phosphatase 1 catalytic (PPP1C) subunits. (genenames.org)
  • The Src homology 2 (SH2) domain-containing protein tyrosine phosphatase, SHP-2, interacts with many proteins by recognizing the tyrosine-phosphorylated Y(I/V)X(L/V/I) motifs through its amino-terminal SH2 domain (for a review, see reference 53 ). (asm.org)
  • Thus, alkaline phosphatase may potentially also hydrolyze phosphate groups of proteins, but we cannot provide any in-house data and procedures concerning dephosphorylation of proteins. (sigmaaldrich.com)
  • In a reverse genetic screen, we identified the chloroplast PP2C phosphatase, PHOTOSYSTEM II CORE PHOSPHATASE (PBCP), which is required for efficient dephosphorylation of PSII proteins. (plantcell.org)
  • It is not yet known whether dephosphorylation of proteins catalyzed by phosphatases occurs in the apoplastic space. (plantphysiol.org)
  • In this study, we found that tobacco ( Nicotiana tabacum ) purple acid phosphatase could dephosphorylate the phosphoryl residues of three apoplastic proteins, two of which were identified as α -xylosidase and β -glucosidase. (plantphysiol.org)
  • Nevertheless, this phosphatase may be involved in the activation of synthases indirectly by acting on either apoplastic proteins or unidentified membrane proteins, since the level of activation for glucan synthases was only a 2- to 3-fold increase in the transgenic tobacco cells overexpressing NtPAP12 compared with wild-type cells. (plantphysiol.org)
  • We compared the influence of the TPR proteins FK506 binding proteins 51 and 52, protein phosphatase-5, C-terminus of Hsp70 interacting protein, cyclophillin 40, hepatitis-virus-B X-associated protein-2, and tetratricopeptide repeat protein-2 on all six steroid hormone receptors in a homogeneous mammalian cell system. (nih.gov)
  • This, combined with the high molar concentrations of these phosphatases found in some cells, makes it sometimes difficult to identify their relative contribution to the dephosphorylation of specific substrates in intact cells through the use of these inhibitors. (sigmaaldrich.com)
  • Total phosphatase extracts from cells are then added to trigger a solid-phase dephosphorylation reaction. (mcponline.org)
  • Both phosphatases, in addition to catalyzing the conversion of phosphorylase a to b, also catalyzed the dephosphorylation of glycogen synthase D, activated phosphorylase kinase, phosphorylated histone, phosphorylated casein, and the phosphorylated inhibitory component of troponin (TN-I). The relative activities of the phosphatases with respect to phosphorylase a, glycogen synthase D, histone, and casein remained essentially constant throughout the purification. (meta.org)
  • In the current study, we have elucidated a mechanism whereby protein phosphatase 2A (PP2A) is activated by a cAMP/PKA-dependent pathway, leading to dephosphorylation of Thr-75. (pnas.org)
  • Through the use of protein phosphatase inhibitors, our results have suggested a mechanism whereby cAMP may activate a PP2A-like protein phosphatase leading to dephosphorylation of Thr-75 of DARPP-32. (pnas.org)
  • Inactivation, or dephosphorylation, of AKT should be regulated by Ser/Thr phosphatases. (aacrjournals.org)
  • However, identity of the phosphatase or phosphatases implicated in AKT dephosphorylation in epithelial malignancies is less clear. (aacrjournals.org)
  • Active Motif's Phosphatase Inhibitor Cocktail is designed to protect phosphoproteins from dephosphorylation during lysis and extraction procedures from mammalian cells or tissues and for immunoprecipitation and kinase assays. (activemotif.com)
  • Dephosphorylation of Rabbit Skeletal Muscle Glycogen Synthase (Phosphorylated by Cyclic AMP-independent Synthase Kinase 1) by Phosphatases. (sigmaaldrich.com)
  • To achieve maximal dephosphorylation, fresh phosphatase was added to the reaction every 3 h to a final concentration of 100 U/ml. (sigmaaldrich.com)
  • Type 2 phosphatases were further divided depending on their divalent cation requirements for full activity: phosphatase 2A (PP2A) does not require such cations, whereas phosphatase 2B (PP2B, also known as calcineurin) and phosphatase 2C (PP2C) are respectively activated by Ca 2+ and Mg 2+ . (sigmaaldrich.com)
  • The tumor suppressor protein phosphatase 2A (PP2A) acts as a negative regulator of these pathways. (nih.gov)
  • Protein phosphatase type 2A (PP2A) enzymes constitute a large family of Ser/Thr phosphatases with multiple functions in cellular signaling and physiology. (nih.gov)
  • In this review, we highlight how PP2A holoenzyme biogenesis and enzymatic activity are controlled by a sophisticatedly coordinated network of five PP2A modulators, consisting of α4, phosphatase 2A phosphatase activator (PTPA), leucine carboxyl methyl transferase 1 (LCMT1), PP2A methyl esterase 1 (PME-1) and, potentially, target of rapamycin signaling pathway regulator-like 1 (TIPRL1), which serve to prevent promiscuous phosphatase activity until the holoenzyme is completely assembled. (nih.gov)
  • The removal of the phosphate is regulated by pSer/pThr-specific phosphatases with the two most prominent ones being PP1 and PP2A. (portlandpress.com)
  • Protein phosphatase 2A (PP2A) is a large family of enzymes that account for the majority of brain Ser/Thr phosphatase activity. (frontiersin.org)
  • The PP2A/Bα isoform binds to tau and is the primary tau phosphatase. (frontiersin.org)
  • The aim of this review is to shed light on the role of four different phosphatases (PTEN, PP2A, CDC25 and DUSP1) in five different solid tumors (breast cancer, lung cancer, pancreatic cancer, prostate cancer and ovarian cancer), in order to better understand the most frequent and aggressive primary cancer of the central nervous system, glioblastoma. (biochemj.org)
  • Hydrolysis of phosphoesters, phosphate transferase activity, protein phosphatase activity, phosphate transport, modulation of organic cation transport, and involvement in cell proliferation have been suggested as possible functions of ALP. (sigmaaldrich.com)
  • Liver (hepatic) cells can consume the glucose-6-phosphate in glycolysis , or remove the phosphate group using the enzyme glucose-6-phosphatase and release the free glucose into the bloodstream for uptake by other cells. (bionity.com)
  • Deregulation and mutations of protein kinases and phosphatases are commonly observed in human diseases, specifically cancer. (grantome.com)
  • Genomic studies have revealed the presence of Ser/Thr kinases and phosphatases in many bacterial species, although their physiological roles have largely been unclear. (asm.org)
  • On the basis of their substrate specificity they are usually divided into phosphoserine and phosphothreonine phosphatases on the one hand, and phosphotyrosine and dual-specificity phosphatases, on the other hand. (sigmaaldrich.com)
  • A study of substrate specificity for a CTD phosphatase, SCP1, by proteomic screening of binding partners. (nih.gov)
  • An emphasis is also placed on the substrate specificity of alkaline phosphatases, their catalytic properties as phosphohydrolases as well as phosphodiesterases and their structural and functional relatedness to a large superfamily of enzymes that includes nucleotide pyrophosphatase/phosphodiesterase. (springer.com)
  • PBCP and STN8 form an antagonistic kinase and phosphatase pair whose substrate specificity and physiological functions are distinct from those of STN7 and the counteracting phosphatase PROTEIN PHOSPHATASE1/THYLAKOID-ASSOCIATED PHOSPHATASE38, but their activities may overlap to some degree. (plantcell.org)
  • Inhibitor of protein-phosphatase 1. (abcam.com)
  • DARPP-32, a dopamine-regulated neuronal phosphoprotein, is a potent inhibitor of protein phosphatase-1. (cornell.edu)
  • The observation that many of the physical and chemical properties of purified DARPP-32 resemble those of phosphatase inhibitor-1 (inhibitor-1), a widely distributed inhibitor of protein phosphatase-1, suggests that DARPP-32 might also function as a phosphatase inhibitor. (cornell.edu)
  • The degree of inhibition for protein, acid and alkaline phosphatase activity was determined in mouse brain extract following treatment with Pierce Phosphatase Inhibitor Tablets or another commercially available phosphatase inhibitor tablet. (thermofisher.com)
  • Alkaline phosphatase (AP) is a non-specific phosphomonoester hydrolase that catalyzes the hydrolysis of a wide variety of organic monophosphates. (sigmaaldrich.com)
  • 0.1 to 0.2 mg/ml of phosphoprotein, and 10U alkaline phosphatase. (sigmaaldrich.com)
  • Alkaline Phosphatase can be inactivated by heat: Heat the reaction for 10 min at +65 °C followed by at least one extraction with phenol/chloroform/isoamylalcohol (50 : 48 : 2). (sigmaaldrich.com)
  • The availability of knockout mice deficient in each of the murine alkaline phosphatase isozymes has also given deep insights into their in vivo role. (springer.com)
  • This has been particularly true for probing the biological role of bone alkaline phosphatase during skeletal mineralization. (springer.com)
  • Summary of the gene nomenclature, accession numbers, common names, tissue distribution and function, if known, for the human and mouse alkaline phosphatase isozymes. (springer.com)
  • Groom LA, Sneddon AA, Alessi DR, Dowd S, Keyse SM: Differential regulation of the MAP, SAP and RK/p38 kinases by Pyst1, a novel cytosolic dual-specificity phosphatase. (hmdb.ca)
  • Dual specificity phosphatase that dephosphorylates MAP kinase MAPK1/ERK2 on both 'Thr-183' and 'Tyr-185', regulating its activity during the meiotic cell cycle (By similarity). (hmdb.ca)
  • Orthologous to human DUSP2 (dual specificity phosphatase 2). (jax.org)
  • Relative levels of total and phosphorylated protein were determined following protein extraction in the absence (-) or presence (+) of phosphatase inhibitors for ( A ) AKT and PDGFR in serum-starved, PDGF-stimulated (100 ng/mL) NIH 3T3 cell extracts and ( B ) ERK1/2 in liver and spleen tissue extracts. (thermofisher.com)
  • Moreover, the selective protein phosphatase 1 and 2A inhibitors okadaic acid and calyculin A prevented the LFS-induced depotentiation. (jneurosci.org)
  • Sensitivity to a panel of phosphatase inhibitors suggests involvement of the phosphatase PP1 in this process. (aacrjournals.org)
  • Since phosphatase levels may vary among cell and tissue types, it may be necessary to increase the concentration of inhibitors. (activemotif.com)
  • Here, we report the design of a quantitative and high-throughput assay platform for monitoring cellular phosphatase activity toward specific phosphoprotein targets. (mcponline.org)
  • After stopping the reaction, phosphoprotein levels are quantified by ELISA with a phospho-specific antibody, and the loss of phospho-specific immunoreactivity is used as the readout of phosphatase activity. (mcponline.org)
  • We illustrate the generality of the method by developing specific phosphatase-activity assays for the three canonical mitogen-activated protein phospho-kinases: ERK, JNK, and p38. (mcponline.org)
  • Cellular PPase activity toward these phosphoprotein subsets is regulated at multiple levels. (mcponline.org)
  • Moreover, we show that the activity of SnRK2s from group 1 is additionally regulated by okadaic acid-sensitive phosphatase(s) from the phosphoprotein phosphatase (PPP) family. (upv.es)
  • Enzyme activity was recovered in the final step as two distinct peaks tentatively referred to as phosphoprotein phosphatases I and II. (meta.org)
  • REST is a bona fide substrate for SCP1 in vivo and that SCP1 phosphatase activity protects REST against degradation. (nih.gov)
  • Title: Phosphatase activity of small C-terminal domain phosphatase 1 (SCP1) controls the stability of the key neuronal regulator RE1-silencing transcription factor (REST). (nih.gov)
  • We describe here a family of protein-aspartate phosphatases with activity on Spo0F approximately P, a response regulator component of the phosphorelay, that provide a mechanism for signal recognition and interpretation. (nih.gov)
  • Moreover, stimulation of protein phosphatase activity by this mechanism may represent an important signaling pathway regulated by cAMP in neurons and other types of cell. (pnas.org)
  • These data suggest that the phosphatase activity of CD148 may be involved in the regulation of T cell activation. (jimmunol.org)
  • These kits are ideal for measuring phosphatase and kinase activity and for monitoring relative phosphoprotein or phosphopeptide concentrations during chromatography or after IEF fractionation of protein samples. (thermofisher.com)
  • Cutting edge: Dependence of TCR antagonism on Src homology 2 domain‐containing protein tyrosine phosphatase activity. (currentprotocols.com)
  • However, the phosphatase is phosphorylated and its activity is suppressed (determined by in vitro assay). (aacrjournals.org)
  • This binding to phosphorylase a prevents any phosphatase activity of PP1 and maintains the glycogen phosphorylase in its active phosphorylated configuration. (wikipedia.org)
  • Researchers at the New York State Institute for Basic Research in Developmental Disabilities showed that there is significantly lower type 1 phosphatase activity in both gray and white matters in Alzheimer disease brains. (wikipedia.org)
  • Functional analysis of gp130 in rat hepatoma cells by using transduced chimeric G-CSFR-gp130 receptor constructs demonstrates that SHP-2, the Src homology 2 (SH2) domain-containing protein tyrosine phosphatase, acts as a negative regulator of the JAK/STAT signaling in part by downregulating JAK activity, thereby indirectly moderating the induction of STAT3-dependent APP genes. (asm.org)
  • This protein-protein interaction enhances the tyrosine phosphatase activity of SHP-2 by relieving the inhibitory intramolecular interaction between the amino-terminal SH2 domain and the catalytic phosphatase domain ( 26 ). (asm.org)
  • The second mechanism is dependent on the substrate binding and/or phosphatase activity of SHP-2 ( 47 , 53 ). (asm.org)
  • GO annotations related to this gene include hydrolase activity and phosphoprotein phosphatase activity . (genecards.org)
  • No. 713 023 , 25 U/ml) combined good phosphatase activity with lack of detectable proteolytic activity towards MAPs. (sigmaaldrich.com)
  • 1. Foulkes, J.G., Howard, R.F. and Ziemiecki, A. Detection of a novel mammalian protein phosphatase with activity for phosphotyrosine. (qmul.ac.uk)
  • Attempted overexpression of the tobacco purple acid phosphatase NtPAP12 in tobacco cells not only decreased the activity levels of the glycosidases but also increased levels of xyloglucan oligosaccharides and cello-oligosaccharides in the apoplast during the exponential phase. (plantphysiol.org)
  • We suggest that purple acid phosphatase controls the activity of α -xylosidase and β -glucosidase, which are responsible for the degradation of xyloglucan oligosaccharides and cello-oligosaccharides in the cell walls. (plantphysiol.org)
  • Exhibits mitogen-activated protein kinase binding activity and phosphoprotein phosphatase activity. (jax.org)
  • These results suggest that IL-6 regulation of APP genes is affected by SHP-2 in two ways: SHP-2 acts as a phosphatase on the JAK/STAT pathway and serves as linker to the MAP kinase pathway, which in turn moderates APP production. (asm.org)
  • Dephosphorylates O- phosphotyrosine groups in phosphoproteins, such as the products of EC EC 2.7.10.2 non-specific protein-tyrosine kinase. (qmul.ac.uk)
  • The head domain contains a large N-terminal extension composed of multiple ankyrin repeats, which are implicated in mediating an association with the protein phosphatase 1 (PP1) catalytic subunits 1α and 1γ. (jneurosci.org)
  • The structural features and restricted expression patterns suggest that members of this novel class of unconventional myosins comprise a mechanism to target selectively the protein phosphatase 1 catalytic subunits 1α and/or 1γ in developing brain. (jneurosci.org)
  • It includes the classic PP2C phosphatases, a number of enzymes recently discovered and pyruvate dehydrogenase phosphatases. (sigmaaldrich.com)
  • The Arabidopsis SERK1 protein interacts with the AAA-ATPase AtCDC48, the 14-3-3 protein GF14lambda and the PP2C phosphatase KAPP. (ebi.ac.uk)
  • Three-dimensional structure of a mammalian purple acid phosphatase at 2.2 A resolution with a mu-(hydr)oxo bridged di-iron center. (ebi.ac.uk)
  • DARPP-32 (dopamine- and cyclic-AMP-regulated phosphoprotein of molecular weight 32,000) is a neuronal phosphoprotein that displays a regional distribution in the mammalian brain very similar to that of dopamine-containing nerve terminals, being highly concentrated in the basal ganglia. (cornell.edu)
  • Thus, the basal ganglia of mammalian brain contain a region-specific neuronal phosphoprotein that is a protein phosphatase inhibitor. (cornell.edu)
  • Due to space constraints this mini-review focuses exclusively on structural and functional features of mammalian alkaline phosphatases as identified by crystallography and probed by site-directed mutagenesis and kinetic analysis. (springer.com)
  • Using a combination of tandem affinity purification tagging and mass spectrometry, we characterized a novel, evolutionarily conserved protein phosphatase 4 (PP4)-containing complex (PP4cs, protein phosphatase 4, cisplatin-sensitive complex) that plays a critical role in the eukaryotic DNA damage response. (mcponline.org)
  • Over the past decade, an understanding of the molecular mechanisms that underlie this versatility has emerged in the case of one of the major eukaryotic protein phosphatases: protein phosphatase 1 (PP1). (biologists.org)
  • Here we review bacterial Ser/Thr kinases (eSTKs) that show homology in their catalytic domains to eukaryotic Ser/Thr kinases and their partner phosphatases (eSTPs) that are homologous to eukaryotic phosphatases. (asm.org)
  • This review focuses primarily on bacterial kinases that show homology in their catalytic domains to eukaryotic Ser/Thr kinases (eSTKs) and, to a lesser extent, on their partner eukaryote-like phosphatases (eSTPs). (asm.org)
  • Protein tyrosine phosphatases in the human genome. (currentprotocols.com)
  • Investigation of protein‐tyrosine phosphatases by in‐gel assays. (currentprotocols.com)
  • Glutathione-Responsive Selenosulfide Prodrugs as a Platform Strategy for Potent and Selective Mechanism-Based Inhibition of Protein Tyrosine Phosphatases. (yale.edu)
  • The phosphoprotein phosphatase(s) acting on muscle phosphorylase a was purified from rabbit liver by acid precipitation, high speed centrifugation, chromatography on DEAE-Sephadex A-50, Sephadex G-75, and Sepharose-histone. (meta.org)
  • Calcineurin is a calcium-dependent, calmodulin-stimulated protein phosphatase involved in the downstream regulation of dopaminergic signal transduction. (genecards.org)
  • This entry represents a group of kinase associated protein phosphatases from plants, including KAPP (also known as protein phosphatase 2C 70) from Arabidopsis. (ebi.ac.uk)
  • Hypersensitive to red and blue 1 and its modification by protein phosphatase 7 are implicated in the control of Arabidopsis stomatal aperture. (biomedsearch.com)
  • 2. Gallis, B., Bornstein, P. and Brautigan, D.L. Tyrosylprotein kinase and phosphatase activities in membrane vesicles from normal and Rous sarcoma virus-transformed rat cells. (qmul.ac.uk)
  • DARPP-32 (dopamine and cyclic AMP-regulated phosphoprotein, relative molecular mass 32,000) is a cytosolic protein highly enriched in medium-sized spiny neurons of the neostriatum (1). (creativebiomart.net)
  • We have recently reported that nicotine stimulates the release of dopamine via α4β2 * nAChRs and/or α7 nAChRs, leading to the regulation of DARPP-32 at Thr34, the site involved in regulation of protein phosphatase-1 (PP-1). (aspetjournals.org)
  • Our discovery and characterization of striatal phosphoproteins controlled by dopamine, including DARPP-32, RCS, and ARPP-16, provides a rational approach to the elucidation of the molecular actions of dopamine. (yale.edu)
  • In addition, we use mouse models where striatal phosphoproteins and their targets have been "knocked out" to investigate the functions of these dopamine-regulated pathways in a variety of behavioral paradigms. (yale.edu)
  • Conclusions: Phosphatase ABI1 and okadaic acid-sensitive phosphatases of the PPP family are negative regulators of salt stress-activated SnRK2.4. (upv.es)
  • In addition to the Pro-Q® Diamond phosphoprotein gel stain, some of our kits include SYPRO Ruby total-protein stain and PeppermintStick™ phosphoprotein molecular weight standards to serve as extra controls in your experiments. (thermofisher.com)
  • Reciprocal regulation of ARPP-16 by PKA and MAST3 kinases provides a cAMP-regulated switch in protein phosphatase 2A inhibition. (yale.edu)
  • This gene encodes a member of the small C-terminal domain phosphatase (SCP) family of nuclear phosphatases. (nih.gov)
  • Structural and functional analysis of the phosphoryl transfer reaction mediated by the human small C-terminal domain phosphatase, Scp1. (nih.gov)
  • Our current studies focus on the biochemical characterization of DARPP-32 and its target, protein phosphatase-1, on RCS and the regulation of calmodulin-dependent signaling, and on ARPP-16 and its potential involvement in regulation of protein phosphatase 2A. (yale.edu)