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 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 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 non-essential amino acid. In animals it is synthesized from PHENYLALANINE. It is also the precursor of EPINEPHRINE; THYROID HORMONES; and melanin.
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 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
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.
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 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.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
Protein kinases that catalyze the PHOSPHORYLATION of TYROSINE residues in proteins with ATP or other nucleotides as phosphate donors.
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 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.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
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.
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 PROTEIN-TYROSINE KINASE family that was originally identified by homology to the Rous sarcoma virus ONCOGENE PROTEIN PP60(V-SRC). They interact with a variety of cell-surface receptors and participate in intracellular signal transduction pathways. Oncogenic forms of src-family kinases can occur through altered regulation or expression of the endogenous protein and by virally encoded src (v-src) genes.
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.
The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.
Proteins that are present in blood serum, including SERUM ALBUMIN; BLOOD COAGULATION FACTORS; and many other types of 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.
Established cell cultures that have the potential to propagate indefinitely.
Transport proteins that carry specific substances in the blood or across cell membranes.
Commonly observed structural components of proteins formed by simple combinations of adjacent secondary structures. A commonly observed structure may be composed of a CONSERVED SEQUENCE which can be represented by a CONSENSUS SEQUENCE.
Proteins prepared by recombinant DNA technology.
The uptake of naked or purified DNA by CELLS, usually meaning the process as it occurs in eukaryotic cells. It is analogous to bacterial transformation (TRANSFORMATION, BACTERIAL) and both are routinely employed in GENE TRANSFER TECHNIQUES.
The sequential correspondence of nucleotides in one nucleic acid molecule with those of another nucleic acid molecule. Sequence homology is an indication of the genetic relatedness of different organisms and gene function.
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.
Membrane-associated tyrosine-specific kinases encoded by the c-src genes. They have an important role in cellular growth control. Truncation of carboxy-terminal residues in pp60(c-src) leads to PP60(V-SRC) which has the ability to transform cells. This kinase pp60 c-src should not be confused with csk, also known as c-src kinase.
Phosphatidylinositols in which one or more alcohol group of the inositol has been substituted with a phosphate group.
A signal transducing adaptor protein that links extracellular signals to the MAP KINASE SIGNALING SYSTEM. Grb2 associates with activated EPIDERMAL GROWTH FACTOR RECEPTOR and PLATELET-DERIVED GROWTH FACTOR RECEPTORS via its SH2 DOMAIN. It also binds to and translocates the SON OF SEVENLESS PROTEINS through its SH3 DOMAINS to activate PROTO-ONCOGENE PROTEIN P21(RAS).
Genetically engineered MUTAGENESIS at a specific site in the DNA molecule that introduces a base substitution, or an insertion or deletion.
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).)
Models used experimentally or theoretically to study molecular shape, electronic properties, or interactions; includes analogous molecules, computer-generated graphics, and mechanical structures.
A phosphoinositide phospholipase C subtype that is structurally defined by the presence of an N-terminal pleckstrin-homology and EF-hand domains, a central catalytic domain, and a C-terminal calcium-dependent membrane-binding domain.
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 subcategory of protein tyrosine phosphatases that contain SH2 type SRC HOMOLOGY DOMAINS. Many of the proteins in this class are recruited to specific cellular targets such as a cell surface receptor complexes via their SH2 domain.
The characteristic 3-dimensional shape of a protein, including the secondary, supersecondary (motifs), tertiary (domains) and quaternary structure of the peptide chain. PROTEIN STRUCTURE, QUATERNARY describes the conformation assumed by multimeric proteins (aggregates of more than one polypeptide chain).
Products of proto-oncogenes. Normally they do not have oncogenic or transforming properties, but are involved in the regulation or differentiation of cell growth. They often have protein kinase activity.
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.
Protein factors that promote the exchange of GTP for GDP bound to GTP-BINDING PROTEINS.
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.
Protein modules with conserved ligand-binding surfaces which mediate specific interaction functions in SIGNAL TRANSDUCTION PATHWAYS and the specific BINDING SITES of their cognate protein LIGANDS.
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.
Screening techniques first developed in yeast to identify genes encoding interacting proteins. Variations are used to evaluate interplay between proteins and other molecules. Two-hybrid techniques refer to analysis for protein-protein interactions, one-hybrid for DNA-protein interactions, three-hybrid interactions for RNA-protein interactions or ligand-based interactions. Reverse n-hybrid techniques refer to analysis for mutations or other small molecules that dissociate known interactions.
A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite.
The level of protein structure in which regular hydrogen-bond interactions within contiguous stretches of polypeptide chain give rise to alpha helices, beta strands (which align to form beta sheets) or other types of coils. This is the first folding level of protein conformation.
A phosphoinositide phospholipase C subtype that is primarily regulated by PROTEIN-TYROSINE KINASES. It is structurally related to PHOSPHOLIPASE C DELTA with the addition of SRC HOMOLOGY DOMAINS and pleckstrin homology domains located between two halves of the CATALYTIC DOMAIN.
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.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Cell lines whose original growing procedure consisted being transferred (T) every 3 days and plated at 300,000 cells per plate (J Cell Biol 17:299-313, 1963). Lines have been developed using several different strains of mice. Tissues are usually fibroblasts derived from mouse embryos but other types and sources have been developed as well. The 3T3 lines are valuable in vitro host systems for oncogenic virus transformation studies, since 3T3 cells possess a high sensitivity to CONTACT INHIBITION.
The relationship between the chemical structure of a compound and its biological or pharmacological activity. Compounds are often classed together because they have structural characteristics in common including shape, size, stereochemical arrangement, and distribution of functional groups.
Proteins which bind to DNA. The family includes proteins which bind to both double- and single-stranded DNA and also includes specific DNA binding proteins in serum which can be used as markers for malignant diseases.
A class of proteins involved in the transport of molecules via TRANSPORT VESICLES. They perform functions such as binding to the cell membrane, capturing cargo molecules and promoting the assembly of CLATHRIN. The majority of adaptor proteins exist as multi-subunit complexes, however monomeric varieties have also been found.
A sequence of amino acids in a polypeptide or of nucleotides in DNA or RNA that is similar across multiple species. A known set of conserved sequences is represented by a CONSENSUS SEQUENCE. AMINO ACID MOTIFS are often composed of conserved sequences.
A non-essential amino acid that is synthesized from GLUTAMIC ACID. It is an essential component of COLLAGEN and is important for proper functioning of joints and tendons.
Serologic tests in which a positive reaction manifested by visible CHEMICAL PRECIPITATION occurs when a soluble ANTIGEN reacts with its precipitins, i.e., ANTIBODIES that can form a precipitate.
A phosphoinositide present in all eukaryotic cells, particularly in the plasma membrane. It is the major substrate for receptor-stimulated phosphoinositidase C, with the consequent formation of inositol 1,4,5-triphosphate and diacylglycerol, and probably also for receptor-stimulated inositol phospholipid 3-kinase. (Kendrew, The Encyclopedia of Molecular Biology, 1994)
A family of high molecular weight GTP phosphohydrolases that play a direct role in vesicle transport. They associate with microtubule bundles (MICROTUBULES) and are believed to produce mechanical force via a process linked to GTP hydrolysis. This enzyme was formerly listed as EC 3.6.1.50.
The degree of similarity between sequences. Studies of AMINO ACID SEQUENCE HOMOLOGY and NUCLEIC ACID SEQUENCE HOMOLOGY provide useful information about the genetic relatedness of genes, gene products, and species.
The degree of 3-dimensional shape similarity between proteins. It can be an indication of distant AMINO ACID SEQUENCE HOMOLOGY and used for rational DRUG DESIGN.
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.
A subclass of phospholipases that hydrolyze the phosphoester bond found in the third position of GLYCEROPHOSPHOLIPIDS. Although the singular term phospholipase C specifically refers to an enzyme that catalyzes the hydrolysis of PHOSPHATIDYLCHOLINE (EC 3.1.4.3), it is commonly used in the literature to refer to broad variety of enzymes that specifically catalyze the hydrolysis of PHOSPHATIDYLINOSITOLS.
A tyrosine-specific protein kinase encoded by the v-src oncogene of ROUS SARCOMA VIRUS. The transforming activity of pp60(v-src) depends on both the lack of a critical carboxy-terminal tyrosine phosphorylation site at position 527, and the attachment of pp60(v-src) to the plasma membrane which is accomplished by myristylation of its N-terminal glycine.
Phosphotransferases that catalyzes the conversion of 1-phosphatidylinositol to 1-phosphatidylinositol 3-phosphate. Many members of this enzyme class are involved in RECEPTOR MEDIATED SIGNAL TRANSDUCTION and regulation of vesicular transport with the cell. Phosphatidylinositol 3-Kinases have been classified both according to their substrate specificity and their mode of action within the cell.
Deletion of sequences of nucleic acids from the genetic material of an individual.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Src-family kinases that associate with T-CELL ANTIGEN RECEPTOR and phosphorylate a wide variety of intracellular signaling molecules.
The process of moving proteins from one cellular compartment (including extracellular) to another by various sorting and transport mechanisms such as gated transport, protein translocation, and vesicular transport.
Partial proteins formed by partial hydrolysis of complete proteins or generated through PROTEIN ENGINEERING techniques.
Proteins that activate the GTPase of specific GTP-BINDING PROTEINS.
The process by which two molecules of the same chemical composition form a condensation product or polymer.
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 group of hydrolases which catalyze the hydrolysis of monophosphoric esters with the production of one mole of orthophosphate. EC 3.1.3.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
Signal transducing adaptor proteins that contain SRC HOMOLOGY DOMAINS and play a role in CYTOSKELETON reorganization. c-crk protein is closely related to ONCOGENE PROTEIN V-CRK and includes several alternatively spliced isoforms.
Retrovirus-associated DNA sequences (src) originally isolated from the Rous sarcoma virus (RSV). The proto-oncogene src (c-src) codes for a protein that is a member of the tyrosine kinase family and was the first proto-oncogene identified in the human genome. The human c-src gene is located at 20q12-13 on the long arm of chromosome 20.
Filamentous proteins that are the main constituent of the thin filaments of muscle fibers. The filaments (known also as filamentous or F-actin) can be dissociated into their globular subunits; each subunit is composed of a single polypeptide 375 amino acids long. This is known as globular or G-actin. In conjunction with MYOSINS, actin is responsible for the contraction and relaxation of muscle.
The rate dynamics in chemical or physical systems.
Process of generating a genetic MUTATION. It may occur spontaneously or be induced by MUTAGENS.
A CELL LINE derived from human T-CELL LEUKEMIA and used to determine the mechanism of differential susceptibility to anti-cancer drugs and radiation.
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.
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 naturally occurring or experimentally induced replacement of one or more AMINO ACIDS in a protein with another. If a functionally equivalent amino acid is substituted, the protein may retain wild-type activity. Substitution may also diminish, enhance, or eliminate protein function. Experimentally induced substitution is often used to study enzyme activities and binding site properties.
The first continuously cultured human malignant CELL LINE, derived from the cervical carcinoma of Henrietta Lacks. These cells are used for VIRUS CULTIVATION and antitumor drug screening assays.
Proto-oncogene proteins that are guanine nucleotide exchange factors for RHO GTPASES. They also function as signal transducing adaptor proteins.
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 family of signaling adaptor proteins that contain SRC HOMOLOGY DOMAINS. Many members of this family are involved in transmitting signals from CELL SURFACE RECEPTORS to MITOGEN-ACTIVATED PROTEIN KINASES.
Extrachromosomal, usually CIRCULAR DNA molecules that are self-replicating and transferable from one organism to another. They are found in a variety of bacterial, archaeal, fungal, algal, and plant species. They are used in GENETIC ENGINEERING as CLONING VECTORS.
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.
Members of the class of compounds composed of AMINO ACIDS joined together by peptide bonds between adjacent amino acids into linear, branched or cyclical structures. OLIGOPEPTIDES are composed of approximately 2-12 amino acids. Polypeptides are composed of approximately 13 or more amino acids. PROTEINS are linear polypeptides that are normally synthesized on RIBOSOMES.
A deoxyribonucleotide polymer that is the primary genetic material of all cells. Eukaryotic and prokaryotic organisms normally contain DNA in a double-stranded state, yet several important biological processes transiently involve single-stranded regions. DNA, which consists of a polysugar-phosphate backbone possessing projections of purines (adenine and guanine) and pyrimidines (thymine and cytosine), forms a double helix that is held together by hydrogen bonds between these purines and pyrimidines (adenine to thymine and guanine to cytosine).
A mutation caused by the substitution of one nucleotide for another. This results in the DNA molecule having a change in a single base pair.
A subtype of dynamin found primarily in the NEURONS of the brain.
Microscopy of specimens stained with fluorescent dye (usually fluorescein isothiocyanate) or of naturally fluorescent materials, which emit light when exposed to ultraviolet or blue light. Immunofluorescence microscopy utilizes antibodies that are labeled with fluorescent dye.
Non-receptor tyrosine kinases encoded by the C-ABL GENES. They are distributed in both the cytoplasm and the nucleus. c-Abl plays a role in normal HEMATOPOIESIS especially of the myeloid lineage. Oncogenic transformation of c-abl arises when specific N-terminal amino acids are deleted, releasing the kinase from negative regulation.
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.
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.
Signaling proteins which function as master molecular switches by activating Rho GTPases through conversion of guanine nucleotides. Rho GTPases in turn control many aspects of cell behavior through the regulation of multiple downstream signal transduction pathways.
Derivatives of phosphatidic acids in which the phosphoric acid is bound in ester linkage to the hexahydroxy alcohol, myo-inositol. Complete hydrolysis yields 1 mole of glycerol, phosphoric acid, myo-inositol, and 2 moles of fatty acids.
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)
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.
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.
Different forms of a protein that may be produced from different GENES, or from the same gene by ALTERNATIVE SPLICING.
Major constituent of the cytoskeleton found in the cytoplasm of eukaryotic cells. They form a flexible framework for the cell, provide attachment points for organelles and formed bodies, and make communication between parts of the cell possible.
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.
Enzymes that hydrolyze GTP to GDP. EC 3.6.1.-.
Proteins found in any species of bacterium.
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.
The biosynthesis of RNA carried out on a template of DNA. The biosynthesis of DNA from an RNA template is called REVERSE TRANSCRIPTION.
A member of the Rho family of MONOMERIC GTP-BINDING PROTEINS. It is associated with a diverse array of cellular functions including cytoskeletal changes, filopodia formation and transport through the GOLGI APPARATUS. This enzyme was formerly listed as EC 3.6.1.47.
PROTEINS that specifically activate the GTP-phosphohydrolase activity of RAS PROTEINS.
A subfamily in the family MURIDAE, comprising the hamsters. Four of the more common genera are Cricetus, CRICETULUS; MESOCRICETUS; and PHODOPUS.
The network of filaments, tubules, and interconnecting filamentous bridges which give shape, structure, and organization to the cytoplasm.
The aggregation of soluble ANTIGENS with ANTIBODIES, alone or with antibody binding factors such as ANTI-ANTIBODIES or STAPHYLOCOCCAL PROTEIN A, into complexes large enough to fall out of solution.
Retroviral proteins that have the ability to transform cells. They can induce sarcomas, leukemias, lymphomas, and mammary carcinomas. Not all retroviral proteins are oncogenic.
This enzyme is a lymphoid-specific src family tyrosine kinase that is critical for T-cell development and activation. Lck is associated with the cytoplasmic domains of CD4, CD8 and the beta-chain of the IL-2 receptor, and is thought to be involved in the earliest steps of TCR-mediated T-cell activation.
Structurally related forms of an enzyme. Each isoenzyme has the same mechanism and classification, but differs in its chemical, physical, or immunological characteristics.
NMR spectroscopy on small- to medium-size biological macromolecules. This is often used for structural investigation of proteins and nucleic acids, and often involves more than one isotope.
A signal transducing adaptor protein that is encoded by the crk ONCOGENE from TYPE C AVIAN RETROVIRUSES. It contains SRC HOMOLOGY DOMAINS and is closely related to its cellular homolog, PROTO-ONCOGENE PROTEIN C-CRK.
CELL LINE derived from the ovary of the Chinese hamster, Cricetulus griseus (CRICETULUS). The species is a favorite for cytogenetic studies because of its small chromosome number. The cell line has provided model systems for the study of genetic alterations in cultured mammalian cells.
A large collection of DNA fragments cloned (CLONING, MOLECULAR) from a given organism, tissue, organ, or cell type. It may contain complete genomic sequences (GENOMIC LIBRARY) or complementary DNA sequences, the latter being formed from messenger RNA and lacking intron sequences.
Proteins coded by oncogenes. They include proteins resulting from the fusion of an oncogene and another gene (ONCOGENE PROTEINS, FUSION).
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
Proteins that originate from insect species belonging to the genus DROSOPHILA. The proteins from the most intensely studied species of Drosophila, DROSOPHILA MELANOGASTER, are the subject of much interest in the area of MORPHOGENESIS and development.
A group of enzymes that catalyzes the phosphorylation of serine or threonine residues in proteins, with ATP or other nucleotides as phosphate donors.
Cellular uptake of extracellular materials within membrane-limited vacuoles or microvesicles. ENDOSOMES play a central role in endocytosis.
The facilitation of a chemical reaction by material (catalyst) that is not consumed by the reaction.
A broad category of proteins involved in the formation, transport and dissolution of TRANSPORT VESICLES. They play a role in the intracellular transport of molecules contained within membrane vesicles. Vesicular transport proteins are distinguished from MEMBRANE TRANSPORT PROTEINS, which move molecules across membranes, by the mode in which the molecules are transported.
A group of enzymes that transfers a phosphate group onto an alcohol group acceptor. EC 2.7.1.
A protein-serine-threonine kinase that is activated by PHOSPHORYLATION in response to GROWTH FACTORS or INSULIN. It plays a major role in cell metabolism, growth, and survival as a core component of SIGNAL TRANSDUCTION. Three isoforms have been described in mammalian cells.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
Proteins which are involved in the phenomenon of light emission in living systems. Included are the "enzymatic" and "non-enzymatic" types of system with or without the presence of oxygen or co-factors.
A characteristic feature of enzyme activity in relation to the kind of substrate on which the enzyme or catalytic molecule reacts.
Processes involved in the formation of TERTIARY PROTEIN STRUCTURE.
Protein interaction domains of about 70-90 amino acid residues, named after a common structure found in PSD-95, Discs Large, and Zona Occludens 1 proteins. PDZ domains are involved in the recruitment and interaction of proteins, and aid the formation of protein scaffolds and signaling networks. This is achieved by sequence-specific binding between a PDZ domain in one protein and a PDZ motif in another protein.
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.
Proteins to which calcium ions are bound. They can act as transport proteins, regulator proteins, or activator proteins. They typically contain EF HAND MOTIFS.
The relationships of groups of organisms as reflected by their genetic makeup.
Electrophoresis in which a polyacrylamide gel is used as the diffusion medium.
Diffusible gene products that act on homologous or heterologous molecules of viral or cellular DNA to regulate the expression of proteins.
Members of the src-family tyrosine kinase family that are strongly expressed in MYELOID CELLS and B-LYMPHOCYTES.
The characteristic 3-dimensional shape and arrangement of multimeric proteins (aggregates of more than one polypeptide chain).
IMMUNOGLOBULINS on the surface of B-LYMPHOCYTES. Their MESSENGER RNA contains an EXON with a membrane spanning sequence, producing immunoglobulins in the form of type I transmembrane proteins as opposed to secreted immunoglobulins (ANTIBODIES) which do not contain the membrane spanning segment.
Proto-oncogene proteins that negatively regulate RECEPTOR PROTEIN-TYROSINE KINASE signaling. It is a UBIQUITIN-PROTEIN LIGASE and the cellular homologue of ONCOGENE PROTEIN V-CBL.
A continuous cell line of high contact-inhibition established from NIH Swiss mouse embryo cultures. The cells are useful for DNA transfection and transformation studies. (From ATCC [Internet]. Virginia: American Type Culture Collection; c2002 [cited 2002 Sept 26]. Available from http://www.atcc.org/)
In vitro method for producing large amounts of specific DNA or RNA fragments of defined length and sequence from small amounts of short oligonucleotide flanking sequences (primers). The essential steps include thermal denaturation of the double-stranded target molecules, annealing of the primers to their complementary sequences, and extension of the annealed primers by enzymatic synthesis with DNA polymerase. The reaction is efficient, specific, and extremely sensitive. Uses for the reaction include disease diagnosis, detection of difficult-to-isolate pathogens, mutation analysis, genetic testing, DNA sequencing, and analyzing evolutionary relationships.
A set of genes descended by duplication and variation from some ancestral gene. Such genes may be clustered together on the same chromosome or dispersed on different chromosomes. Examples of multigene families include those that encode the hemoglobins, immunoglobulins, histocompatibility antigens, actins, tubulins, keratins, collagens, heat shock proteins, salivary glue proteins, chorion proteins, cuticle proteins, yolk proteins, and phaseolins, as well as histones, ribosomal RNA, and transfer RNA genes. The latter three are examples of reiterated genes, where hundreds of identical genes are present in a tandem array. (King & Stanfield, A Dictionary of Genetics, 4th ed)
A high molecular weight (220-250 kDa) water-soluble protein which can be extracted from erythrocyte ghosts in low ionic strength buffers. The protein contains no lipids or carbohydrates, is the predominant species of peripheral erythrocyte membrane proteins, and exists as a fibrous coating on the inner, cytoplasmic surface of the membrane.
Molecules on the surface of T-lymphocytes that recognize and combine with antigens. The receptors are non-covalently associated with a complex of several polypeptides collectively called CD3 antigens (ANTIGENS, CD3). Recognition of foreign antigen and the major histocompatibility complex is accomplished by a single heterodimeric antigen-receptor structure, composed of either alpha-beta (RECEPTORS, ANTIGEN, T-CELL, ALPHA-BETA) or gamma-delta (RECEPTORS, ANTIGEN, T-CELL, GAMMA-DELTA) chains.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
Common name for the species Gallus gallus, the domestic fowl, in the family Phasianidae, order GALLIFORMES. It is descended from the red jungle fowl of SOUTHEAST ASIA.
The sum of the weight of all the atoms in a molecule.
A mammalian homolog of the DROSOPHILA SON OF SEVENLESS PROTEIN. It is a guanine nucleotide exchange factor for RAS PROTEINS.
Proteins found in any species of fungus.
A binding partner for several RECEPTOR PROTEIN-TYROSINE KINASES, including INSULIN RECEPTOR and INSULIN-LIKE GROWTH FACTOR RECEPTOR. It contains a C-terminal SH2 DOMAIN and mediates various SIGNAL TRANSDUCTION pathways.
A cell surface receptor involved in regulation of cell growth and differentiation. It is specific for EPIDERMAL GROWTH FACTOR and EGF-related peptides including TRANSFORMING GROWTH FACTOR ALPHA; AMPHIREGULIN; and HEPARIN-BINDING EGF-LIKE GROWTH FACTOR. The binding of ligand to the receptor causes activation of its intrinsic tyrosine kinase activity and rapid internalization of the receptor-ligand complex into the cell.
A biosensing technique in which biomolecules capable of binding to specific analytes or ligands are first immobilized on one side of a metallic film. Light is then focused on the opposite side of the film to excite the surface plasmons, that is, the oscillations of free electrons propagating along the film's surface. The refractive index of light reflecting off this surface is measured. When the immobilized biomolecules are bound by their ligands, an alteration in surface plasmons on the opposite side of the film is created which is directly proportional to the change in bound, or adsorbed, mass. Binding is measured by changes in the refractive index. The technique is used to study biomolecular interactions, such as antigen-antibody binding.
Glycoproteins found on the membrane or surface of cells.
A superfamily of PROTEIN-SERINE-THREONINE KINASES that are activated by diverse stimuli via protein kinase cascades. They are the final components of the cascades, activated by phosphorylation by MITOGEN-ACTIVATED PROTEIN KINASE KINASES, which in turn are activated by mitogen-activated protein kinase kinase kinases (MAP KINASE KINASE KINASES).
A cell line generated from human embryonic kidney cells that were transformed with human adenovirus type 5.
A subclass of myosins found generally associated with actin-rich membrane structures such as filopodia. Members of the myosin type I family are ubiquitously expressed in eukaryotes. The heavy chains of myosin type I lack coiled-coil forming sequences in their tails and therefore do not dimerize.
Proteins which maintain the transcriptional quiescence of specific GENES or OPERONS. Classical repressor proteins are DNA-binding proteins that are normally bound to the OPERATOR REGION of an operon, or the ENHANCER SEQUENCES of a gene until a signal occurs that causes their release.
Use of restriction endonucleases to analyze and generate a physical map of genomes, genes, or other segments of DNA.
Regulatory proteins that act as molecular switches. They control a wide range of biological processes including: receptor signaling, intracellular signal transduction pathways, and protein synthesis. Their activity is regulated by factors that control their ability to bind to and hydrolyze GTP to GDP. EC 3.6.1.-.
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)
A 6-kDa polypeptide growth factor initially discovered in mouse submaxillary glands. Human epidermal growth factor was originally isolated from urine based on its ability to inhibit gastric secretion and called urogastrone. Epidermal growth factor exerts a wide variety of biological effects including the promotion of proliferation and differentiation of mesenchymal and EPITHELIAL CELLS. It is synthesized as a transmembrane protein which can be cleaved to release a soluble active form.
A genetic rearrangement through loss of segments of DNA or RNA, bringing sequences which are normally separated into close proximity. This deletion may be detected using cytogenetic techniques and can also be inferred from the phenotype, indicating a deletion at one specific locus.
A structurally-related group of signaling proteins that are phosphorylated by the INSULIN RECEPTOR PROTEIN-TYROSINE KINASE. The proteins share in common an N-terminal PHOSPHOLIPID-binding domain, a phosphotyrosine-binding domain that interacts with the phosphorylated INSULIN RECEPTOR, and a C-terminal TYROSINE-rich domain. Upon tyrosine phosphorylation insulin receptor substrate proteins interact with specific SH2 DOMAIN-containing proteins that are involved in insulin receptor signaling.
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)
A cell line derived from cultured tumor cells.
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.
A rac GTP-binding protein involved in regulating actin filaments at the plasma membrane. It controls the development of filopodia and lamellipodia in cells and thereby influences cellular motility and adhesion. It is also involved in activation of NADPH OXIDASE. This enzyme was formerly listed as EC 3.6.1.47.
Structures which are part of the CELL MEMBRANE or have cell membrane as a major part of their structure.
Adherence of cells to surfaces or to other cells.
A genus of small, two-winged flies containing approximately 900 described species. These organisms are the most extensively studied of all genera from the standpoint of genetics and cytology.
Processes that stimulate the GENETIC TRANSCRIPTION of a gene or set of genes.
A process whereby multiple RNA transcripts are generated from a single gene. Alternative splicing involves the splicing together of other possible sets of EXONS during the processing of some, but not all, transcripts of the gene. Thus a particular exon may be connected to any one of several alternative exons to form a mature RNA. The alternative forms of mature MESSENGER RNA produce PROTEIN ISOFORMS in which one part of the isoforms is common while the other parts are different.
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.
A microfilament protein that interacts with F-ACTIN and regulates cortical actin assembly and organization. It is also an SH3 DOMAIN containing phosphoprotein, and it mediates tyrosine PHOSPHORYLATION based SIGNAL TRANSDUCTION by PROTO-ONCOGENE PROTEIN PP60(C-SRC).
Detection of RNA that has been electrophoretically separated and immobilized by blotting on nitrocellulose or other type of paper or nylon membrane followed by hybridization with labeled NUCLEIC ACID PROBES.
Catalyzes the ATP-dependent PHOSPHORYLATION of GMP to generate GDP and ADP.
A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.
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.
MONOMERIC GTP-BINDING PROTEINS that were initially recognized as allosteric activators of the MONO(ADP-RIBOSE) TRANSFERASE of the CHOLERA TOXIN catalytic subunit. They are involved in vesicle trafficking and activation of PHOSPHOLIPASE D. This enzyme was formerly listed as EC 3.6.1.47
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 multistage process that includes cloning, physical mapping, subcloning, determination of the DNA SEQUENCE, and information analysis.
A CELL LINE derived from a PHEOCHROMOCYTOMA of the rat ADRENAL MEDULLA. PC12 cells stop dividing and undergo terminal differentiation when treated with NERVE GROWTH FACTOR, making the line a useful model system for NERVE CELL differentiation.
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.
Elements of limited time intervals, contributing to particular results or situations.
A light microscopic technique in which only a small spot is illuminated and observed at a time. An image is constructed through point-by-point scanning of the field in this manner. Light sources may be conventional or laser, and fluorescence or transmitted observations are possible.
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 sub-family of RHO GTP-BINDING PROTEINS that is involved in regulating the organization of cytoskeletal filaments. This enzyme was formerly listed as EC 3.6.1.47.

Cryo-electron microscopy structure of an SH3 amyloid fibril and model of the molecular packing. (1/3051)

Amyloid fibrils are assemblies of misfolded proteins and are associated with pathological conditions such as Alzheimer's disease and the spongiform encephalopathies. In the amyloid diseases, a diverse group of normally soluble proteins self-assemble to form insoluble fibrils. X-ray fibre diffraction studies have shown that the protofilament cores of fibrils formed from the various proteins all contain a cross-beta-scaffold, with beta-strands perpendicular and beta-sheets parallel to the fibre axis. We have determined the threedimensional structure of an amyloid fibril, formed by the SH3 domain of phosphatidylinositol-3'-kinase, using cryo-electron microscopy and image processing at 25 A resolution. The structure is a double helix of two protofilament pairs wound around a hollow core, with a helical crossover repeat of approximately 600 A and an axial subunit repeat of approximately 27 A. The native SH3 domain is too compact to fit into the fibril density, and must unfold to adopt a longer, thinner shape in the amyloid form. The 20x40-A protofilaments can only accommodate one pair of flat beta-sheets stacked against each other, with very little inter-strand twist. We propose a model for the polypeptide packing as a basis for understanding the structure of amyloid fibrils in general.  (+info)

Socs1 binds to multiple signalling proteins and suppresses steel factor-dependent proliferation. (2/3051)

We have identified Socs1 as a downstream component of the Kit receptor tyrosine kinase signalling pathway. We show that the expression of Socs1 mRNA is rapidly increased in primary bone marrow-derived mast cells following exposure to Steel factor, and Socs1 inducibly binds to the Kit receptor tyrosine kinase via its Src homology 2 (SH2) domain. Previous studies have shown that Socs1 suppresses cytokine-mediated differentiation in M1 cells inhibiting Janus family kinases. In contrast, constitutive expression of Socs1 suppresses the mitogenic potential of Kit while maintaining Steel factor-dependent cell survival signals. Unlike Janus kinases, Socs1 does not inhibit the catalytic activity of the Kit tyrosine kinase. In order to define the mechanism by which Socs1-mediated suppression of Kit-dependent mitogenesis occurs, we demonstrate that Socs1 binds to the signalling proteins Grb-2 and the Rho-family guanine nucleotide exchange factors Vav. We show that Grb2 binds Socs1 via its SH3 domains to putative diproline determinants located in the N-terminus of Socs1, and Socs1 binds to the N-terminal regulatory region of Vav. These data suggest that Socs1 is an inducible switch which modulates proliferative signals in favour of cell survival signals and functions as an adaptor protein in receptor tyrosine kinase signalling pathways.  (+info)

Anopheles gambiae Ag-STAT, a new insect member of the STAT family, is activated in response to bacterial infection. (3/3051)

A new insect member of the STAT family of transcription factors (Ag-STAT) has been cloned from the human malaria vector Anopheles gambiae. The domain involved in DNA interaction and the SH2 domain are well conserved. Ag-STAT is most similar to Drosophila D-STAT and to vertebrate STATs 5 and 6, constituting a proposed ancient class A of the STAT family. The mRNA is expressed at all developmental stages, and the protein is present in hemocytes, pericardial cells, midgut, skeletal muscle and fat body cells. There is no evidence of transcriptional activation following bacterial challenge. However, bacterial challenge results in nuclear translocation of Ag-STAT protein in fat body cells and induction of DNA-binding activity that recognizes a STAT target site. In vitro treatment with pervanadate (vanadate and H2O2) translocates Ag-STAT to the nucleus in midgut epithelial cells. This is the first evidence of direct participation of the STAT pathway in immune responses in insects.  (+info)

DEF-1, a novel Src SH3 binding protein that promotes adipogenesis in fibroblastic cell lines. (4/3051)

The Src homology 3 (SH3) motif is found in numerous signal transduction proteins involved in cellular growth and differentiation. We have purified and cloned a novel protein, DEF-1 (differentiation-enhancing factor), from bovine brain by using a Src SH3 affinity column. Ectopic expression of DEF-1 in fibroblasts resulted in the differentiation of a significant fraction of the culture into adipocytes. This phenotype appears to be related to the induction of the transcription factor peroxisome proliferator-activated receptor gamma (PPARgamma), since DEF-1 NIH 3T3 cells demonstrated augmented levels of PPARgamma mRNA and, when treated with activating PPARgamma ligands, efficient induction of differentiation. Further evidence for a role for DEF-1 in adipogenesis was provided by heightened expression of DEF-1 mRNA in adipose tissue isolated from obese and diabetes mice compared to that in tissue isolated from wild-type mice. However, DEF-1 mRNA was detected in multiple tissues, suggesting that the signal transduction pathway(s) in which DEF-1 is involved is not limited to adipogenesis. These results suggest that DEF-1 is an important component of a signal transduction process that is involved in the differentiation of fibroblasts and possibly of other types of cells.  (+info)

Identification of a new Pyk2 target protein with Arf-GAP activity. (5/3051)

Protein tyrosine kinase Pyk2 is activated by a variety of G-protein-coupled receptors and by extracellular signals that elevate intracellular Ca2+ concentration. We have identified a new Pyk2 binding protein designated Pap. Pap is a multidomain protein composed of an N-terminal alpha-helical region with a coiled-coil motif, followed by a pleckstrin homology domain, an Arf-GAP domain, an ankyrin homology region, a proline-rich region, and a C-terminal SH3 domain. We demonstrate that Pap forms a stable complex with Pyk2 and that activation of Pyk2 leads to tyrosine phosphorylation of Pap in living cells. Immunofluorescence experiments demonstrate that Pap is localized in the Golgi apparatus and at the plasma membrane, where it is colocalized with Pyk2. In addition, in vitro recombinant Pap exhibits strong GTPase-activating protein (GAP) activity towards the small GTPases Arf1 and Arf5 and weak activity towards Arf6. Addition of recombinant Pap protein to Golgi preparations prevented Arf-dependent generation of post-Golgi vesicles in vitro. Moreover, overexpression of Pap in cultured cells reduced the constitutive secretion of a marker protein. We propose that Pap functions as a GAP for Arf and that Pyk2 may be involved in regulation of vesicular transport through its interaction with Pap.  (+info)

Granulocyte-macrophage colony-stimulating factor-activated signaling pathways in human neutrophils. Involvement of Jak2 in the stimulation of phosphatidylinositol 3-kinase. (6/3051)

Granulocyte-macrophage colony-stimulating factor (GM-CSF) regulates many of the biological activities of human neutrophils. The signaling pathways via which these effects are mediated are not fully understood. We have shown previously that GM-CSF treatment of human neutrophils activates the Janus kinase/signal transducers and activators of transcription (Jak/STAT) pathway and, more specifically, Jak2, STAT3, and STAT5B in neutrophils. GM-CSF also stimulates the activity of the phosphatidylinositol 3-kinase (PI3-kinase) in a tyrosine kinase-dependent manner. Here we report that pretreating the cells with a Jak2 inhibitor (AG-490) abolishes tyrosine phosphorylation of the p85 subunit of PI3-kinase induced by GM-CSF. Furthermore, p85 was found to associate with Jak2, but not with Lyn, in stimulated cells in situ and with its autophosphorylated form in vitro; however, Jak2 did not bind to either of the two Src homology 2 (SH2) domains of the p85 subunit of PI3-kinase. Although STAT5B bound to the carboxyl-terminal SH2 domain of p85, it was absent from the complex containing PI3-kinase and Jak2. These results suggest that stimulation of the activity of PI3-kinase induced by GM-CSF is mediated by Jak2 and that the association between Jak2 and p85 depends on an adaptor protein yet to be identified.  (+info)

C-terminal Src kinase associates with ligand-stimulated insulin-like growth factor-I receptor. (7/3051)

Increased expression of the insulin-like growth factor-I receptor (IGF-IR) protein-tyrosine kinase occurs in several kinds of cancer and induces neoplastic transformation in fibroblast cell lines. The transformed phenotype can be reversed by interfering with the function of the IGF-IR. The IGF-IR is required for transformation by a number of viral and cellular oncoproteins, including SV40 large T antigen, Ras, Raf, and Src. The IGF-IR is a substrate for Src in vitro and is phosphorylated in v-Src-transformed cells. We observed that the IGF-IR and IR associated with the C-terminal Src kinase (CSK) following ligand stimulation. We found that the SH2 domain of CSK binds to the tyrosine-phosphorylated form of IGF-IR and IR. We determined the tyrosine residues in the IGF-IR and in the IR responsible for this interaction. We also observed that fibroblasts stimulated with IGF-I or insulin showed a rapid and transient decrease in c-Src tyrosine kinase activity. The results suggest that c-Src and CSK are involved in IGF-IR and IR signaling and that the interaction of CSK with the IGF-IR may play a role in the decrease in c-Src activity following IGF-I stimulation.  (+info)

Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter protein having similar binding and biological properties to Nck. (8/3051)

Adapter proteins made up of Src homology (SH) domains mediate multiple cellular signaling events initiated by receptor protein tyrosine kinases. Here we report that Grb4 is an adapter protein closely related to but distinct from Nck that is made up of three SH3 domains and one SH2 domain. Northern analysis indicated that both genes are expressed in multiple tissues. Both Nck and Grb4 proteins could associate with receptor tyrosine kinases and the SH3-binding proteins PAK, Sos1, and PRK2, and they synergized with v-Abl and Sos to induce gene expression via the transcription factor Elk-1. Although neither protein was transforming on its own, both Nck and Grb4 cooperated with v-Abl to transform NIH 3T3 cells and influenced the morphology and anchorage-dependent growth of wild type Ras-transformed cells. Nck and Grb4 therefore appear to be functionally redundant.  (+info)

The MLL gene, the closest human homologue to the Drosophila trithorax gene, undergoes chromosomal translocation with a large number of different partner genes in both acute lymphoid and acute myeloid leukemias. We have identified a new partner gene, EEN, fused to MLL in a case of acute myeloid leukemia. The gene is located on chromosome 19p13, where two other MLL partner genes, ENL and ELL/MEN have also been identified. The deduced protein of 368 aa contains a central α-helical region and a C-terminal Src homology 3 (SH3) domain most similar to the C-terminal SH3 domain found in the Grb2/Sem-5/Drk family of genes. Sequence analysis of the fusion MLL/EEN transcript in our patient reveals that exon 6 of MLL is fused to the N- terminal end of EEN, a fusion that would create a chimeric protein that includes the major functional domain of EEN. EEN is expressed in a variety of tissue types and encodes a protein of approximately 46 kDa. The EEN protein is the human homologue of a member of a recently ...
フィンガープリント Comparison of the frequency of functional SH3 domains with different limited sets of amino acids using mRNA display の研究トピックを掘り下げます。これらはともに一意のフィンガープリントを構成します。 ...
Receptor tyrosine kinases (RTKs) control a host of biological functions by phosphorylating tyrosine residues of intracellular proteins upon extracellular ligand binding. The phosphotyrosines (p-Tyr) then recruit a subset of ∼100 Src homology 2 (SH2) domain-containing proteins to the cell membrane. The in vivo kinetics of this process are not well understood. Here we use total internal reflection (TIR) microscopy and single-molecule imaging to monitor interactions between SH2 modules and p-Tyr sites near the cell membrane. We found that the dwell time of SH2 modules within the TIR illumination field is significantly longer than predictions based on chemical dissociation rate constants, suggesting that SH2 modules quickly rebind to nearby p-Tyr sites after dissociation. We also found that, consistent with the rebinding model, the effective diffusion constant is negatively correlated with the respective dwell time for different SH2 domains and the dwell time is positively correlated with the local
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Phospholipase C (PLC)-gamma is unique among the PLC enzymes because each PLC-gamma isozyme contains a split pleckstrin homology (PH) domain with an SH2SH2SH3 tandem repeat insertion (where SH indicates Src homology domain) in the middle of its sequence. Split PH domains exist in a number of other proteins that play crucial signaling roles. However, little is known about the structure and function of split PH domains. The C-terminal half of the PLC-gamma split PH domain has been implicated to interact directly with the TRPC3 calcium channel, thereby providing a direct coupling mechanism between PLC-gamma and agonist-induced calcium entry. However, this interaction has not been proved by direct biochemical or structural studies. Here we determined the three-dimensional structure of the split PH domain of PLC-gamma1, and we found that the split PH domain of the enzyme folds into a canonical PH domain fold with high thermostability. The SH2SH2SH3 insertion between the beta3 and beta4 strands does ...
In light of the Scansite prediction and these data, we tested the potential of these proteins to interact with an inactive mutant of caspase-8-to prevent apoptosis induction-in transfected cells. P85 strongly interacted with caspase-8 ( Fig. 2B). This interaction depended on the integrity of the Y380 site but was independent of another phosphorylation site, Y334, identified independently by proteomics ( 12). The interaction was also dependent on cotransfected, activated c-src (Y527F or Δ92-95) or c-fyn (Y531F), which were more effective than wild-type c-src or kinase-inactive c-src (K295M). The phosphorylation of caspase-8 by these src constructs correlated with the magnitude of the caspase-8-p85 interaction. Deletion of the COOH-terminal SH2 domain of p85 abolished the interaction ( Fig. 2C), implicating this SH2 domain in the caspase-8 interaction. Other candidates identified from the Panomics screen (Nck-2, c-fyn, SHP-2) interacted more weakly or independently of phosphorylation ...
oriented toward one of the stimulus sh, and the distance to this sh was set at 14, 16, 18, 22, and 28 cm. Following the light stimulus, test sh were again released and observed. Krause and Tegeder hypothesized that sh would approach the neighbor that they could reach in the shortest amount of time, even if that meant turning toward the second sh and approaching it. This hypothesis held true in the experiment, as test sh took time to turn and approach their nearer neighbor if it would take less time than swimming straight toward a farther sh. It should be noted that sh did not always turn toward the closer neighbor, but this behavior became more probable as distance increased (Figure 10). !In the nal experiment, the time-minimization hypothesis was tested using 5 free-swimming sh in a test pool. Fish were given time to acclimate and spread out before the light stimulus was introduced. Immediately following the stimulus, sh executed behavior known as a #C-start, a short-term predator evasion reex ...
src/tests/netns.sh , 40 ++++++++++++++++++++++++++++++++++++++++ 1 file changed, 40 insertions(+) diff --git a/src/tests/netns.sh b/src/tests/netns.sh index 568612c..4cfcf61 100755 --- a/src/tests/netns.sh +++ b/src/tests/netns.sh @@ -222,6 +222,46 @@ n1 wg set wg0 peer $more_specific_key remove ip1 link del wg0 ip2 link del wg0 +# Test using transit namespace. We now change the topology to this with transit-net of wg0 = $ns0 +# ┌──────────────────────┐ ┌───────────────────────┐ ┌────────────────────────────────────────┐ +# │ $ns1 namespace │ │ $ns0 namespace │ │ $ns2 namespace │ +# │ │ │ │ │ │ +# │ ┌─────┐ │ │ ┌──────┐ │ │ ┌─────┐ ┌─────┐ │ +# │ │ wg0 │ │ │ ...
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Vitamina B1,roli i vitamines B1,vitaminat b1,vitamina,vitaminat,rendesia e vitamines B1,vitamina b1 shqip,vitaminat shqip,vitamina shqip Shëndetësi, Vitaminat, Vitamina B1, Tiamina, Karboksilaza, Kokarboksilaza, Oksidimi, Acidi piruvik, Dekarboksilimi, Karbohidratet, Acidi laktik,
SH2B adapter protein 3 (SH2B3), also known as lymphocyte adapter protein (LNK), is a protein that in humans is encoded by the SH2B3 gene on chromosome 12. SH2B adapter protein 3 is a protein that in humans is encoded by the SH2B3 gene on chromosome 12. It is ubiquitously expressed in many tissues and cell types. LNK functions as a regulator in signaling pathways relating to hematopoiesis, inflammation, and cell migration. As a result, it is involved in blood diseases, autoimmune disorders, and vascular disease. The SH2B3 gene also contains one of 27 SNPs associated with increased risk of coronary artery disease. The SH2B3 gene resides on chromosome 12 at the band 12q24 and contains 12 exons. This protein belongs to the Src homology 2-B (SH2B) adapter family. LNK contains 3 functional domains: a C-terminal Src homology 2 (SH2) domain, a pleckstrin homology (PH) domain, and a dimerization domain. The SH2 domain spans approximately 100 amino acid residues and binds phosphotyrosine-containing ...
DescriptionThe Crk family of adaptor proteins is ubiquitously expressed in most tissues and mediates the timely formation of protein complexes elicited by a variety of extracellular stimuli, including various growth and differentiation factors. This class of proteins lacks an apparent catalytic domain and may serve as adaptors, coupling different proteins of a signal transduction cascade. Crk adaptor proteins are made up of one modular Src homology 2 (SH2) and two Src homology 3 (SH3) domains. SH2 domains bind to phosphotyrosine (pTyr) containing sequence, while SH3 domain binds to proline rich motifs. The two SH3 domains are separated by long linker containing highly conserved proline reisdues. Although the role of SH2 and N-terminal SH3 (SH3N) domains of Crk has been generally delineated, the role of C-terminal SH3 (SH3C) domain remains entirely unknown. There is, however, increasing evidence that the SH3C domain along with the linker act as a regulatory element. Despite the fact that Crk has ...
Endocytosis is a fundamental process in signaling and membrane trafficking. The formation of vesicles at the plasma membrane is mediated by the G protein dynamin that catalyzes the final fission step, the actin cytoskeleton, and proteins that sense or induce membrane curvature. One such protein, the F-BAR domain-containing protein pacsin, contributes to this process and has been shown to induce a spectrum of membrane morphologies, including tubules and tube constrictions in vitro. Full-length pacsin isoform 1 (pacsin-1) has reduced activity compared to its isolated F-BAR domain, implicating an inhibitory role for its C-terminal Src homology 3 (SH3) domain. Here we show that the autoinhibitory, intramolecular interactions in pacsin-1 can be released upon binding to the entire proline-rich domain (PRD) of dynamin-1, resulting in potent membrane deformation activity that is distinct from the isolated F-BAR domain. Most strikingly, we observe the generation of small, homogenous vesicles with the activated
The SH2 domain-containing inositol 5-phosphatase (SHIP) recruits the p85 subunit of phosphoinositide 3-kinase during FcγRIIb1-mediated inhibition of B cell receptor signaling Academic Article ...
BioAssay record AID 242624 submitted by ChEMBL: Inhibition of fluorescent (GpYEEI) binding to Src protein tyrosine kinase SH2 domain.
A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is specifically expressed in the brain Academic Article ...
The structure and function of the nervous system is dependent on highly coordinated patterns of migrating neurons. This patterning in many neuronal tissues, including the cortex and retina, results in cell lamination that is essential for proper function of the tissue. Adaptor proteins CT10 regulator of kinase (CRK) and CRK-like are known to be important for proper migration of neurons in the developing cortex through their role in the Reelin signaling pathway. We use Danio rerio, or Zebrafish, as a model organism to study the role of Crk and Crkl in the developing retina. Previous data from our lab have demonstrated that deficiency of Crk and Crkl during development negatively impacts eye size and retinal lamination in Zebrafish. To study the mechanism responsible for this phenotype, we used immunohistochemistry to label proliferating cells in the retina of Crk-deficient, Crkl-deficient, and Crk- and Crkl-deficient embryos at various developmental stages. We hypothesized that Crk- and Crkl-deficient
Proteins encoding phosphotyrosine binding (PTB) domains function as adaptors or scaffolds to organize the signaling complexes involved in wide-ranging physiological processes including neural development, immunity, tissue homeostasis and cell growth. Due to structural differences, PTB domains are divided into three groups represented by phosphotyrosine-dependent IRS-like, phosphotyrosine-dependent Shc-like (see ,PDOC00907,), and phosphotyrosine-independent Dab-like PTBs (see ,PDOC00907,). IRS-type PTB domain has an average length of about 100 amino acids. It binds to the insulin receptor through the Asn-Pro-Xaa-Tyr(P) motif found in many tyrosine-phosphorylated proteins. This domain is found in IRS/Dok/SNT proteins that are the major adapters for RTK and cytokine signaling. This domain binds both peptides and headgroups of phosphatidylinositides, utilizing two distinct binding motifs to mediate spatial organization and localization within cells. The IRS-type PTB domain is found alone or in ...
The learncoil program is a general iterative method that extends the two-stranded coiled coil prediction program paircoil to the identification of other types of coiled coils. Previously, the learncoil program successfully identified three-stranded coiled coils (24).. Iterative approaches similar to learncoil have been applied to sequence alignment and motif recognition (16, 37-41). Each method repeats two steps. First, a scoring algorithm is used to scan a database of sequences for regions thought to represent the motif of interest. Second, selected residues are used to update the parameters of the scoring algorithm (e.g., a weight matrix, profile, or probability table). The updated parameters change the regions identified in the next iteration, and usually these two steps are repeated until convergence occurs.. learncoil combines several strategies to achieve good performance without identifying false-positive sequences (24). First, instead of choosing all sequences that score above a cutoff, ...
Fingerprint Dive into the research topics of Upregulation of immunoregulatory Src homology 2 molecule containing inositol phosphatase and mononuclear cell hyporesponsiveness in oral mucosa during chronic periodontitis. Together they form a unique fingerprint. ...
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Epstein-Barrウイルス(EBV)はヘルペスウイルス群に属し,感染後潜在化し,一生を終わる.免疫抑制剤などで再活性化し,生体に重篤な状態を起こす.EBV関連疾患群である難病の病態に再活性化を起こし関与している可能性がある.関節リウマチ(RA)滑膜炎でのEBVの関与について最初に述べ,根治的治療の可能性について考察する.新たな治療戦略のキーワードは我々が発見し,クローニングしたSAP (signaling lymphocytic-activation molecule associated protein)または,SH2D1A (Src homology 2 domain-containing protein)である.SAP (SH2D1A)はSrc homology 2 (SH2)を持つアダプター分子として免疫細胞で働き,EBVの感染防御,液性免疫に深く関与し,SLEの原因遺伝子としても注目されている.SAP遺伝子の異常はEBVの致死的な感染を起こすX-linked lymphoproliferative (XLP) syndrome (Duncan ...
We report a general method for light-assisted control of interactions of PDZ domain binding motifs with their cognate domains by the incorporation of a photolabile caging group onto the essential C-terminal carboxylate binding determinant of the motif. The strategy was implemented and validated for both simple monovalent and biomimetic divalent ligands, which have recently been established as powerful tools for acute perturbation of native PDZ domain-dependent interactions in live cells ...
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May play a role in signaling pathways governing cellular proliferation, cell growth and differentiation. May be a component of a novel signaling pathway downstream of Shc. Acts as a positive regulator of FGF signaling in neural progenitor cells ...
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TAB2, a novel adaptor protein, mediates activation of TAK1 MAPKKK by linking TAK1 to TRAF6 in the IL-1 signal transduction pathway ...
Mouse polyclonal antibody raised against a full-length human SH2D2A protein. SH2D2A (AAH12107, 1 a.a. ~ 389 a.a) full-length human protein. (H00009047-B01P) - Products - Abnova
Mouse polyclonal antibody raised against a full-length human SH2D3A protein. SH2D3A (AAH06281, 1 a.a. ~ 576 a.a) full-length human protein. (H00010045-B01P) - Products - Abnova
Complete information for SH3BGRL gene (Protein Coding), SH3 Domain Binding Glutamate Rich Protein Like, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
MEGRSAAAETFVWVNNASAHSQSVAKAKYEFLFGRSEGKAPDTSDHGGSTLLPPNVTNEFPEYGTMEEGG 1 - 70 EGLRASLEFDGEALPCHPQEQQGVQPLTGCHSGLDSVTEGPKDVREAPSQSHLKEQSLQPIDSLISALKA 71 - 140 TEARIISGTLQATKVLDQDAVSSFSVQQVEKELDTASRKTQRVNKTLPAGQKNLPEIPLSAEVTTEESFY 141 - 210 LSIQKDLTALLTGDTQAEISQIMNNGRKGAVCVQEPSCPLASLGSSAVTCHSAGSVGFLKEQRSALGREH 211 - 280 PGGCDRSSSMGRPGRVKHVEFQGVEILWTGGDKRETQHPIDFETSLQRTASPDSKESSKVPRHLISSAGL 281 - 350 CNSSSLTENVWDESWKAPSERPGTSSGTFSPVRLDESGEDEVFLQENKQHLEKTPKPERDRERISEQEEH 351 - 420 VKGEDEDILGPGYTEDSTDVYSSQFETILDNTSLYYSAESLETLYSEPDSYFSFEMPLTPMIQQRIKEGG 421 - 490 QFLERTSGGGHQDILSVSADGGIVMGYSSGVTNGLNDASDSIYTKGTPEIAFWGSNAGVKTTRLEAHSEM 491 - 560 GSTEILEKETPENLSNGTSSNVEAAKRLAKRLYQLDRFKRSDVAKHLGKNNEFSKLVAEEYLKFFDFTGM 561 - 630 TLDQSLRYFFKAFSLVGETQERERVLIHFSNRYFYCNPDTIASQDGVHCLTCAIMLLNTDLHGHVNIGKK 631 - 700 MTCQEFIANLQGVNEGVDFSKDLLKALYNSIKNEKLEWAVDDEEKKKSPSESTEEKANGTHPKTISRIGS 701 - 770 TTNPFLDIPHDPNAAVYKSGFLARKIHADMDGKKTPRGKRGWKTFYAVLKGTVLYLQKDEYKPEKALSEE 771 - 840 ...
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Activation of cytoplasmic tyrosine kinase activity is required for T cell receptor (TCR)-dependent lymphocyte activation (1). Adapter proteins serve as substrates for these kinases and as such may function to couple the TCR with downstream signaling events (2-6). SLP-76 is a hematopoietic cell-specific adapter protein that is phosphorylated rapidly on NH2-terminal tyrosine residues after TCR ligation (3), providing a binding site for the Src homology 2 (SH2) domain of Vav (7). SLP-76 also contains a central proline-rich region that associates constitutively with the SH3 domains of Grb2 (8). In addition, SLP-76 has a COOH-terminal SH2 domain that inducibly associates with SLAP-130 (SLP-76-associated phosphoprotein of 130 kD) and an unidentified 62-kD tyrosine phosphoprotein (5, 8, 9). The ability of SLP-76 to augment TCR-dependent nuclear factor of activated T cells (NFAT) activation when transiently overexpressed in a T cell line is dependent on the presence of each of these domains, suggesting ...
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family; C-terminal Src kinase (Csk) subfamily; catalytic (c) domain. The Csk subfamily is composed of Csk, Chk, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk subfamily kinases are cytoplasmic (or nonreceptor) tyr kinases containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr ...
Catalytic domain of C-terminal Src kinase-like Protein Tyrosine Kinases. Protein Tyrosine Kinase (PTK) family; C-terminal Src kinase (Csk) subfamily; catalytic (c) domain. The Csk subfamily is composed of Csk, Chk, and similar proteins. The PTKc family is part of a larger superfamily that includes the catalytic domains of other kinases such as protein serine/threonine kinases, RIO kinases, and phosphoinositide 3-kinase (PI3K). PTKs catalyze the transfer of the gamma-phosphoryl group from ATP to tyrosine (tyr) residues in protein substrates. Csk subfamily kinases are cytoplasmic (or nonreceptor) tyr kinases containing the Src homology domains, SH3 and SH2, N-terminal to the catalytic tyr kinase domain. They negatively regulate the activity of Src kinases that are anchored to the plasma membrane. To inhibit Src kinases, Csk and Chk are translocated to the membrane via binding to specific transmembrane proteins, G-proteins, or adaptor proteins near the membrane. Csk catalyzes the tyr ...
Chronic myeloid leukemia is characterized by the Philadelphia (Ph1) translocation t(9;22) that generates a hybrid gene, bcr/abl, translated to a Mr210,000 tyrosine kinase (p210bcr/abl) with transforming activity for hematopoietic cells. Hematopoietic cell transformation by p210bcr/abl seems to involve activation of the Ras signaling pathway by at least two different signaling intermediates, growth factor receptor-bound protein 2 and Src homology and collagen protein, but additional signaling proteins are likely to be required as well. In an effort to identify additional phosphoproteins activated by p210bcr/abl, we studied the murine, interleukin 3-dependent, myeloid cell line, 32D, and a bcr/abl-transfected, factor-independent subline, 32Dp210. The analysis of whole-cell lysates of 32D and 32Dp210 cells showed that several proteins with a molecular weight of Mr50,000-60,000 were phosphorylated on tyrosine residues in 32Dp210 cells. Because Src family kinases have an apparent molecular weight of ...
Adapter molecule crk also known as proto-oncogene c-Crk or p38 is a protein that in humans is encoded by the CRK gene. The CRK protein participates in the Reelin signaling cascade downstream of DAB1. Adapter molecule crk is a member of an adapter protein family that binds to several tyrosine-phosphorylated proteins. This protein has several SH2 and SH3 domains (src-homology domains) and is involved in several signaling pathways, recruiting cytoplasmic proteins in the vicinity of tyrosine kinase through SH2-phosphotyrosine interaction. The N-terminal SH2 domain of this protein functions as a positive regulator of transformation whereas the C-terminal SH3 domain functions as a negative regulator of transformation. Two alternative transcripts encoding different isoforms with distinct biological activity have been described. Crk together with CrkL participates in the Reelin signaling cascade downstream of DAB1. v-Crk, a transforming oncoprotein from avian sarcoma viruses, is a fusion of viral gag ...
The Src homology 2 (SH2) domain is a protein interaction domain (PID) contained within SRC and other intracellular signal-transducing proteins, many of which drive tumorigenesis, which mediates protein-protein interactions via the docking of SH2 domain-containing proteins to phosphotyrosine (pY) residues on other proteins. Membrane lipids have recently been shown to regulate protein-protein interactions mediated by a different PID and to bind to several SH2 domains. To elucidate the role of lipids in SH2 domain-mediated protein-protein interactions and signal transduction, Park, Sheng, Silkov, Jung, and colleagues performed surface plasmon resonance analysis to systematically characterize the binding affinities of 76 of the 121 known SH2 domains for plasma membrane (PM)-mimetic vesicles which recapitulate the lipid profile of cytofacial PM. Sixty-eight out of the 76 SH2 domains analyzed exhibited moderately high to high levels of affinity for PM-mimetic vesicles. Twelve of 18 SH2 domains ...
The findings presented here support a role for the RhoGEF Trio in axon outgrowth and guidance in mammals. We show that Trio and DCC interact in the embryonic brain, most likely independently of netrin-1. Coexpression of DCC and Trio with Nck-1 and PAK1 suggests that the Trio-DCC interaction probably occurs via the interaction of Trio with PAK1. Furthermore, the N terminus region of Trio comprising the Sec-14 and the spectrin domains mediates the interaction with PAK1. However, it still remains to be determined whether the interaction between Trio and PAK1 is direct. Altogether, these data are consistent with the results obtained in D. melanogaster, where D-Trio genetically interacts with DOCK, PAK, and Rac in controlling axon guidance of photoreceptors (36). Since Nck-1 binds to DCC through its first and third SH3 domains (27) and PAK1 binds to the second SH3 domain of Nck-1 (8), it is tempting to postulate that a cascade of molecular events implicating Nck-1-PAK interaction serves to bridge ...
Resveratrol (trans-3,5,4-truhydroxystilbene) Possesses A Strong Anticancer Activity Exhibited As The Induction Of Apoptosis Through P53 Activation. However, The Molecular Mechanism And Direct Target(s) Of Resveratrol-induced P53 Activation Remain
Predicted to have protein kinase inhibitor activity. Predicted to be involved in intracellular signal transduction and negative regulation of protein tyrosine kinase activity. Predicted to localize to cytoplasm. Is expressed in adaxial cell and myotome. Orthologous to human SH3BP5L (SH3 binding domain protein 5 like ...
1IJR: A novel phosphotyrosine mimetic 4-carboxymethyloxy-3-phosphonophenylalanine (Cpp): exploitation in the design of nonpeptide inhibitors of pp60(Src) SH2 domain.
Complete information for SH2B1 gene (Protein Coding), SH2B Adaptor Protein 1, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
Version-Release number of selected component: gnome-shell-3.18.1-1.fc23 Additional info: reporter: libreport-2.6.3 backtrace_rating: 4 cmdline: /usr/bin/gnome-shell crash_function: js::gc::Cell::arenaHeader executable: /usr/bin/gnome-shell global_pid: 3534 kernel: 4.2.5-300.fc23.x86_64 runlevel: N 5 type: CCpp uid: 1000 Truncated backtrace: Thread no. 1 (10 frames) #0 js::gc::Cell::arenaHeader at /usr/src/debug/mozjs-24.2.0/js/src/gc/Heap.h:947 #1 js::gc::Cell::tenuredZone at /usr/src/debug/mozjs-24.2.0/js/src/gc/Heap.h:994 #2 js::Shape::zone at /usr/src/debug/mozjs-24.2.0/js/src/vm/Shape.h:831 #3 js::ObjectImpl::zone at /usr/src/debug/mozjs-24.2.0/js/src/vm/ObjectImpl-inl.h:360 #4 MarkInternal,JSObject, at /usr/src/debug/mozjs-24.2.0/js/src/gc/Marking.cpp:185 #5 js::gc::MarkKind at /usr/src/debug/mozjs-24.2.0/js/src/gc/Marking.cpp:385 #6 MarkValueInternal at /usr/src/debug/mozjs-24.2.0/js/src/gc/Marking.cpp:505 #7 js::gc::MarkValueRoot at /usr/src/debug/mozjs-24.2.0/js/src/gc/Marking.cpp:528 #8 ...
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SH 34 Study Goals. The goal of the study is to evaluate existing SH 34 and other options identified in the surrounding area of SH 34 in order to better serve the community. Along with partners, we are evaluating:. ...
mouse Sh3md2 protein: scaffold protein that contains four SH3 domains; binds Rac; overexpression induces apoptosis in fibroblasts; RefSeq NM_021506
The domain property of the Document interface gets/sets the domain portion of the origin of the current document, as used by the same origin policy.
Frenchsys, Elitt and SRC found the EPayStandards Consortium, a cooperation for consulting and support of the European payment traffic.
В этом обзоре проанализированы два трансдукционных сигнальных пути, вызываемые активацией глутаматных рецепторов N-метил-D-аспартата (НМДА). Первый путь - ионотропный, обусловлен открытием катионных каналов рецепторов при совпадении деполяризации постсинаптической мембраны, устраняющей магниевый блок катионных каналов, и пресинаптического высвобождения глутамата. В этих условиях в цитоплазму нейрона поступают Са2+, которые активируют Са-зависимые протеинкиназы (СаМКII, ПКА, ПКС, Src) или протеинфосфатазы (РР1, РР2В). Киназы и фосфатазы меняют ...
2fpe: Conserved dimerization of the ib1 src-homology 3 domain *. 2fpf: Crystal structure of the ib1 sh3 dimer at low resolution ... 2fpd: Sad structure determination: crystal structure of the intrinsic dimerization sh3 domain of the ib1 scaffold protein ... 2002). "Jun NH2-terminal kinase (JNK) interacting protein 1 (JIP1) binds the cytoplasmic domain of the Alzheimer's beta-amyloid ...
"Identification of Itk/Tsk Src homology 3 domain ligands". The Journal of Biological Chemistry. 271 (41): 25646-56. doi:10.1074/ ... "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Molecular and Cellular Biology ... a C-terminal VCA domain and central B and GBD (GTP binding domain) domains. WASp, is expressed exclusively in hematopoietic ... of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains". The ...
"Specificity of the binding of synapsin I to Src homology 3 domains". The Journal of Biological Chemistry. 275 (38): 29857-67. ... a middle clathrin and adaptor binding domain and a C-terminal SH3 domain. In the brain, its primary function is thought to be ... "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding ... "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding ...
The JH3-JH4 domains of JAKs share homology with Src-homology-2 (SH2) domains. The amino terminal (NH2) end (JH4-JH7) of Jaks is ... JAKs range from 120-140 kDa in size and have seven defined regions of homology called Janus homology domains 1 to 7 (JH1-7). ... This domain may be involved in regulating the activity of JH1, and was likely a duplication of the JH1 domain which has ... JH2 is a "pseudokinase domain", a domain structurally similar to a tyrosine kinase and essential for a normal kinase activity, ...
Xu J, Ziemnicka D, Merz GS, Kotula L (2001). "Human spectrin Src homology 3 domain binding protein 1 regulates macropinocytosis ... "Identification of a candidate human spectrin Src homology 3 domain-binding protein suggests a general mechanism of association ...
Ye ZS, Baltimore D (1995). "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proc. Natl. Acad. Sci. U.S. ... Ye ZS, Baltimore D (Dec 1994). "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proc. Natl. Acad. Sci. ... "Interleukin 3 and erythropoietin induce association of Vav with Tec kinase through Tec homology domain". Oncogene. 11 (4): 619- ... Katzav S, Cleveland JL, Heslop HE, Pulido D (1991). "Loss of the amino-terminal helix-loop-helix domain of the vav proto- ...
"5-Lipoxygenase contains a functional Src homology 3-binding motif that interacts with the Src homology 3 domain of Grb2 and ... Ye ZS, Baltimore D (December 1994). "Binding of Vav to Grb2 through dimerization of Src homology 3 domains". Proceedings of the ... Okkenhaug K, Rottapel R (August 1998). "Grb2 forms an inducible protein complex with CD28 through a Src homology 3 domain- ... Braverman LE, Quilliam LA (February 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter ...
He identified the phosphotyrosine-binding Src homology 2 (SH2 domain) as the prototypic non-catalytic interaction module. SH2 ... Moran, M. F. (1990). "Src Homology Region 2 Domains Direct Protein-Protein Interactions in Signal Transduction". Proceedings of ... Since the discovery of SH2 domains, hundreds of different modules have been identified in many proteins. Born in Maidstone, ... Pawson, T.; Nash, P. (2003). "Assembly of Cell Regulatory Systems Through Protein Interaction Domains". Science. 300 (5618): ...
Leto TL, Adams AG, de Mendez I (1994). "Assembly of the phagocyte NADPH oxidase: binding of Src homology 3 domains to proline- ... "Specificity of the binding of synapsin I to Src homology 3 domains". J. Biol. Chem. 275 (38): 29857-67. doi:10.1074/jbc. ... Finan PM, Hall A, Kellie S (1996). "Sam68 from an immortalised B-cell line associates with a subset of SH3 domains". FEBS Lett ... bind to moesin through their PX domain". Biochem. Biophys. Res. Commun. 289 (2): 382-8. doi:10.1006/bbrc.2001.5982. PMID ...
Musacchio, A; Noble, M; Pauptit, R; Wierenga, R; Saraste, M (Oct 29, 1992). "Crystal structure of a Src-homology 3 (SH3) domain ... "Structure of the pleckstrin homology domain from beta-spectrin". Nature. 369 (6482): 675-7. Bibcode:1994Natur.369..675M. doi: ... contributing to the determination of the first crystallographic structures of the SH3 and PH domains. During his post-doctoral ... "Modular assembly of RWD domains on the Mis12 complex underlies outer kinetochore organization". Molecular Cell. 53 (4): 591-605 ...
... possible involvement of Src homology 2 domains". J. Cereb. Blood Flow Metab. 19 (8): 880-8. doi:10.1097/00004647-199908000- ... "The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases". J. Biol. Chem. 276 (20): 17199-205. ... "Identification of Itk/Tsk Src homology 3 domain ligands". J. Biol. Chem. 271 (41): 25646-56. doi:10.1074/jbc.271.41.25646. PMID ... "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. 15 (10): 5725 ...
"Identification of Itk/Tsk Src homology 3 domain ligands". The Journal of Biological Chemistry. 271 (41): 25646-56. doi:10.1074/ ... RNA binding protein domains in other proteins that are similar to the RNA binding domain of protein K are called K-homology or ... July 1994). "Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains". Molecular ... The protein encoded by this gene is located in the nucleoplasm and has three repeats of KH domains that binds to RNAs. It is ...
Src homology 3) SH2 - (Src homology 2) C-terminus - tyrosine kinase, catalytic domain ITK (gene) has been shown to interact ... pleckstrin homology domain) TH - Tec family homology domain (including Bruton's tyrosine kinase Cys-rich motif and Proline rich ... Shim EK, Moon CS, Lee GY, Ha YJ, Chae SK, Lee JR (2004). "Association of the Src homology 2 domain-containing leukocyte ... Bunnell SC, Henry PA, Kolluri R, Kirchhausen T, Rickles RJ, Berg LJ (1996). "Identification of Itk/Tsk Src homology 3 domain ...
"Identification of Itk/Tsk Src homology 3 domain ligands". The Journal of Biological Chemistry. 271 (41): 25646-56. doi:10.1074/ ... "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Molecular and Cellular Biology ... a C-terminal VCA domain and central B and GBD (GTP binding domain) domains. WASp, is expressed exclusively in hematopoietic ... WAML (WASP and MIM like), WAWH (WASP without WH1 domain), and WHIMP (WAVE Homology in Membrane Protrusions) have more recently ...
Alexandropoulos K, Cheng G, Baltimore D (1995). "Proline-rich sequences that bind to Src homology 3 domains with individual ... This allows SRC or SRC family kinase to bind NEDD9 via its SH2 domain. Phosphorylation of the NEDD9 substrate domain by Src and ... "Direct binding of the proline-rich region of protein tyrosine phosphatase 1B to the Src homology 3 domain of p130(Cas)". J. ... which contains a Src homology 3 domain and associates with Fyn". Oncogene. 11 (11): 2331-8. PMID 8570184. ...
This gene encodes a Src homology 2 domain-binding protein 1-like protein. The encoded protein interacts with heat shock 70 kDa ... v t e This article incorporates text from the United States National Library of Medicine, which is in the public domain.. ...
"Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Molecular and Cellular Biology ... of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains" (PDF). The ... a PTK domain, and SH2 and SH3 domains which are involved in mediating protein-protein interactions with phosphotyrosine- ... This gene is a member of the Src family of protein tyrosine kinases (PTKs). The encoded protein contains N-terminal sites for ...
Shim EK, Moon CS, Lee GY, Ha YJ, Chae SK, Lee JR (September 2004). "Association of the Src homology 2 domain-containing ... Braverman LE, Quilliam LA (February 1999). "Identification of Grb4/Nckbeta, a src homology 2 and 3 domain-containing adapter ... "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. 15 (10): 5725 ... "Wiskott-Aldrich syndrome protein physically associates with Nck through Src homology 3 domains". Mol. Cell. Biol. 15 (10): 5725 ...
1994). "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem. 269 (8): 5489-92. PMID 8119878 ... binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain". Proc. Natl. Acad. Sci. U.S.A. 94 (16): ... "Association of Ash/Grb-2 with dynamin through the Src homology 3 domain". J. Biol. Chem. 269 (8): 5489-92. PMID 8119878. Sastry ... 1997). "The SH3 domain of amphiphysin binds the proline-rich domain of dynamin at a single site that defines a new SH3 binding ...
1996). "Identification of Itk/Tsk Src homology 3 domain ligands". J. Biol. Chem. 271 (41): 25646-56. doi:10.1074/jbc.271.41. ... 1994). "Identification of Src, Fyn, and Lyn SH3-binding proteins: implications for a function of SH3 domains". Mol. Cell. Biol ... Sam68 (the Src-Associated substrate in Mitosis of 68 kDa) is officially called KHDRBS1 (KH domain containing, RNA binding, ... This gene encodes a member of the K homology domain-containing, RNA-binding, signal transduction-associated protein family. The ...
"Sequences surrounding the Src-homology 3 domain of phospholipase Cgamma-1 increase the domain's association with Cbl". ... "Nerve growth factor binds to the 140 kd trk proto-oncogene product and stimulates its association with the src homology domain ... "Tyrosine phosphorylation of tub and its association with Src homology 2 domain-containing proteins implicate tub in ... tandem SH2 domains, and an SH3 domain.[10] The SH2 domains bind phosphorylated tyrosine residues on target proteins via their ...
"TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm ... But due the high homology between the TEAD family members its believed that TEAD proteins may share cofactors. Here are ... SRF (Serum response factor) and TEAD2 interact through their DNA binding domain, respectively the MADS domain and the TEA ... "TEAD/TEF transcription factors utilize the activation domain of YAP65, a Src/Yes-associated protein localized in the cytoplasm ...
Calponin homology (CH) domain, which is an F-actin binding motif; Src homology 2 (SH2) domain, which mediate interaction with ... Protein domains enriched in the adhesome include: Pleckstrin homology (PH) and FERM domains, which target proteins to the ... examined the effect of inhibition of myosin contractility on the integrin adhesome composition and found LIM domain proteins ... The adhesome contains multi domain proteins with various functions, some of which are specifically enriched in the adhesome ...
"Phosphopeptide selective coordination complexes as promising SRC homology 2 domain mimetics." Inorganic Chemistry. 2012 Aug 6; ... "Progress towards the development of SH2 domain inhibitors." Chemical Society Review. 2013 Apr 21;42(8):3337-70. Drewry JA, ...
... a novel adaptor protein with two Eps15 homology and five Src homology 3 domains". The Journal of Biological Chemistry. 273 (47 ... Sengar AS, Wang W, Bishay J, Cohen S, Egan SE (Mar 1999). "The EH and SH3 domain Ese proteins regulate endocytosis by linking ... Okamoto M, Schoch S, Südhof TC (Jun 1999). "EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin ... Okamoto M, Schoch S, Südhof TC (Jun 1999). "EHSH1/intersectin, a protein that contains EH and SH3 domains and binds to dynamin ...
Gigoux V, L'Hoste S, Raynaud F, Camonis J, Garbay C (2002). "Identification of Aurora kinases as RasGAP Src homology 3 domain- ... The family members have highly conserved C-terminal catalytic domains. Their N-terminal domains, however, exhibit a large ...
This gene encodes a protein with src homology domain 3 (SH3) patterns. Mutations in this gene cause familial juvenile ... "A novel gene that encodes a protein with a putative src homology 3 domain is a candidate gene for familial juvenile ... Donaldson JC, Dise RS, Ritchie MD, Hanks SK (Aug 2002). "Nephrocystin-conserved domains involved in targeting to epithelial ... Donaldson JC, Dise RS, Ritchie MD, Hanks SK (Aug 2002). "Nephrocystin-conserved domains involved in targeting to epithelial ...
"Entrez Gene: SHC3 SHC (Src homology 2 domain containing) transforming protein 3". Nakamura T, Komiya M, Sone K, Hirose E, Gotoh ... "A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is ... Miyake I, Hakomori Y, Misu Y, Nakadate H, Matsuura N, Sakamoto M, Sakai R (April 2005). "Domain-specific function of ShcC ... Their differential regional expression in the brain and roles in neurotrophin and Src signaling". The Journal of Biological ...
"Entrez Gene: SHC2 SHC (Src homology 2 domain containing) transforming protein 2". Warner, A J; Lopez-Dee J; Knight E L; ... Their differential regional expression in the brain and roles in neurotrophin and Src signaling". J Biol Chem. 273 (12): 6960-7 ... SHC2 has been shown to interact with Kinase insert domain receptor. GRCh38: Ensembl release 89: ENSG00000129946 - Ensembl, May ... Kavanaugh WM; Williams LT (Jan 1995). "An alternative to SH2 domains for binding tyrosine-phosphorylated proteins". Science. ...
Zhang H, Gallo KA (2002). "Autoinhibition of mixed lineage kinase 3 through its Src homology 3 domain". J. Biol. Chem. 276 (49 ... a novel src-homology 3 domain-containing proline-rich kinase with serine/threonine kinase activity". J. Biol. Chem. 269 (21): ... identification of a widely-expressed protein kinase bearing an SH3 domain and a leucine zipper-basic region domain". Oncogene. ... This kinase contains a SH3 domain and a leucine zipper-basic motif. This kinase preferentially activates MAPK8/JNK kinase, and ...
Fyn associates with the pICD-TrkB through its Src homology domain 2 (SH2) and is phosphorylated at its Y416 site.[47][48] Once ... Iwasaki Y, Gay B, Wada K, Koizumi S (July 1998). "Association of the Src family tyrosine kinase Fyn with TrkB". Journal of ... BDNF signaling leads to the autophosphorylation of the intracellular domain of the TrkB receptor (ICD-TrkB). Upon ... domain which regulates their capping activity.[58] BDNF can reduce capping activities by upregulating PKC, which can bind to ...
"Functional requirements for interactions between CD84 and Src homology 2 domain-containing proteins and their contribution to ...
The sequential and functional homology of TNF and LT led to the renaming of TNF as TNFα (this article) and LT as TNFβ. In 1985 ... This dissociation enables the adaptor protein TRADD to bind to the death domain, serving as a platform for subsequent protein ... SRC- Vav- Rac axis activates MLK2/MLK3 and these kinases phosphorylate MKK7, which then activates JNK. JNK translocates to the ... The binding of TNF to its receptor and its displacement by LT confirmed the functional homology between the two factors. ...
Because of the high degree of homology in interaction domains and some identified common partners, CASS4 is likely to share ... this motif is conserved among the other three CAS family proteins and is an important binding site for the Src SH2 domain.[11] ... Figure 1. Interaction network and domain structure scheme of Cass4. SH3 domain (SH3) preceded by a short region with no defined ... domain.[8] For the better studied members of the CAS family (BCAR1 and NEDD9), all of these domains have been defined as ...
Lck - a Src family kinase associated with the intracellular tail of CD4 that phosphorylates CD3 and ζ ITAMs of the TCR complex ... The variable domain of both the TCR α-chain and β-chain each have three hypervariable or complementarity determining regions ( ... "A human T cell-specific cDNA clone encodes a protein having extensive homology to immunoglobulin chains". Nature. 308 (5955): ... FYN - a Src family kinase that phosphorylates CD3 and ζ ITAMs. *CD45 - a transmembrane protein whose intracellular tail ...
"5-Lipoxygenase contains a functional Src homology 3-binding motif that interacts with the Src homology 3 domain of Grb2 and ... A PLAT domain within its C2-like domain; this domain, by analogy to other PLAT domain-bearing proteins, may serve as a mobile ... VanderNoot VA, Fitzpatrick FA (1995). "Competitive binding assay of src homology domain 3 interactions between 5-lipoxygenase ... A C-terminal catalytic domain (residues 126-673). *An N-terminal C2-like domain which promotes its binding to ligand substrates ...
Human SRC-1 (steroid receptor coactivator-1) is known to interact with p300/CBP and PCAF, and its HAT domain is located in its ... ACTR (also known as RAC3, AIB1, and TRAM-1 in humans) shares significant sequence homology with SRC-1, in particular in the N- ... It has four functional domains, including an N-terminal domain, a highly conserved catalytic (HAT) domain, an Ada2 interaction ... the HAT domain shows no sequence homology to other known HATs,[7] and it is required for p300/CBP to function in ...
... src homology 2 domain containing)-transforming protein 2 (SHC2) gene: discordant loss in monozygotic twins and frequent loss in ...
... tyrosine kinase receptors and Src homology 3 domain proteins". Oncogene 10 (8): 1475-83. PMID 7537362. ... "Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, ... Yan KS, Kuti M, Yan S, Mujtaba S, Farooq A, Goldfarb MP, Zhou MM (May 2002). "FRS2 PTB domain conformation regulates ... "Structural basis of SNT PTB domain interactions with distinct neurotrophic receptors". Mol. Cell 6 (4): 921-9. PMID 11090629. ...
... s (GPCRs), also known as seven-(pass)-transmembrane domain receptors, 7TM receptors, heptahelical ... Despite the lack of sequence homology between classes, all GPCRs have a common structure and mechanism of signal transduction. ... Another target of c-SRC are the dynamin molecules involved in endocytosis. Dynamins polymerize around the neck of an incoming ... When the receptor is inactive, the GEF domain may be bound to an also inactive α-subunit of a heterotrimeric G-protein. These " ...
"Direct association between the Ret receptor tyrosine kinase and the Src homology 2-containing adapter protein Grb7". J. Biol. ... Common to each isoform is a domain structure. Each protein is divided into three domains: an N-terminal extracellular domain ... a hydrophobic transmembrane domain and a cytoplasmic tyrosine kinase domain, which is split by an insertion of 27 amino acids. ... The extracellular domain of RET contains nine N-glycosylation sites. The fully glycosylated RET protein is reported to have a ...
... possible involvement of Src homology 2 domains". J. Cereb. Blood Flow Metab. (UNITED STATES) 19 (8): 880-8. ISSN 0271-678X. ... tyrosine kinase receptors and Src homology 3 domain proteins". Oncogene (ENGLAND) 10 (8): 1475-83. ISSN 0950-9232. PMID 7537362 ... "Molecular interactions of the Src homology 2 domain protein Shb with phosphotyrosine residues, ... of regions of the Wiskott-Aldrich syndrome protein responsible for association with selected Src homology 3 domains". J. Biol. ...
The N-terminal domain shows homology not only among members of the Hsp90 chaperone family but also to members of the ATPase/ ... Another important role of Hsp90 in cancer is the stabilization of mutant proteins such as v-Src, the fusion oncogene Bcr/Abl, ... that connects the N-terminus with the middle domain a middle domain (MD) of ~40 kDa a C-terminal domain (CTD) of ~12 kDa. ... Hsp90 consists of four structural domains: a highly conserved N-terminal domain (NTD) of ~25 kDa a "charged linker" region, ...
... domain and an SH3 (src homology 3) domain. The guanylate kinase domain of the β subunit binds to the α1 subunit I-II ... the Alpha Interaction Domain, AID) and a region on the GK domain of the β subunit (Alpha Interaction Domain Binding Pocket) was ... The 4-domain architecture (and several key regulatory sites, such as the EF hand and IQ domain at the C-terminus) is also ... The transmembrane helices from the 4 domains line up to form the channel proper; S5 and S6 helices are thought to line the ...
GPCR receptori mogu da samostalno prenose signal posredstvom više tipova proteina, kao što su β-arestin, GRK, i Src. Osim toga ... Gu Q, Ding YS, Zhang TL (May 2010). "Prediction of G-Protein-Coupled Receptor Classes in Low Homology Using Chou's pseudo amino ... "A G protein-coupled receptor with a lipid kinase domain is involved in cell-density sensing". Curr Biol 17 (10): 892-7. PMID ... Još jedna meta c-SRC kinaze su dinamin molekuli koji učestvuju u endocitozi. Dinamini se polimerizuju oko vrata ulazećih ...
Src Homology 3 binding motif).[5][14] Following the SH3-BM is a TAD (transcription activation domain) and a PDZ domain-binding ... YAP1 was first identified by virtue of its ability to associate with the SH3 domain of Yes and Src protein tyrosine kinases.[5] ... Cloning of the YAP1 gene facilitated the identification of a modular protein domain, known as the WW domain.[8][9][10] Two ... which differed by the presence of an extra 38 amino acids that encoded the WW domain.[11][12] Apart from the WW domain, the ...
Mikhalap SV, Shlapatska LM, Berdova AG, Law CL, Clark EA, Sidorenko SP (1999). "CDw150 associates with src-homology 2- ... "Novel mode of ligand binding by the SH2 domain of the human XLP disease gene product SAP/SH2D1A". Curr. Biol. 9 (23): 1355-62. ... "Distinct interactions of the X-linked lymphoproliferative syndrome gene product SAP with cytoplasmic domains of members of the ... "Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells". EMBO J. 20 (21 ...
... domain and an SH3 (src homology 3) domain. The guanylate kinase domain of the β subunit binds to the α1 subunit I-II ... the Alpha Interaction Domain, AID) and a region on the GK domain of the β subunit (Alpha Interaction Domain Binding Pocket) was ... The 4-domain architecture (and several key regulatory sites, such as the EF hand and IQ domain at the C-terminus) is also ... A total of ten α1 subunits that have been identified in humans:[1] α1 subunit contains 4 homologous domains (labeled I-IV), ...
... binding partners for synaptojanin and dynamin via a Grb2-like Src homology 3 domain". Proc. Natl. Acad. Sci. U.S.A. 94 (16): ... "EEN encodes for a member of a new family of proteins containing an Src homology 3 domain and is the third gene located on ... "Src homology 3-domain growth factor receptor-bound 2-like (endophilin) interacting protein 1, a novel neuronal protein that ... SH3GL3, CNSA3, EEN-B2, HsT19371, SH3D2C, SH3P13, SH3 domain containing GRB2 like endophilin A3, SH3 domain containing GRB2 like ...
... and epidermal growth factor receptor via the Grb10 Src homology 2 (SH2) domain and a second novel domain located between the ... pleckstrin homology and SH2 domains". J. Biol. Chem. (UNITED STATES) 273 (12): 6860-7. ISSN 0021-9258. PMID 9506989. doi: ... C-src tirosinska kinaza,[10] EHD1,[11] Cbl genom,[12] RAS p21 proteinskim aktivatorom 1,[3] IRS1,[2][6][13] ARHGEF12,[14] YWHAE ... Arbet-Engels, C; Tartare-Deckert S, Eckhart W (February 1999). "C-terminal Src kinase associates with ligand-stimulated insulin ...
SH2-domænet (efter Src Homology 2) findes i Src-onkoproteinet og mange andre proteiner i signaltransduktionen. SH2-domæner ... Det fosfolipid-bindende PH-domæne (efter Pleckstrin homology domain) er et domæne bestående af omkring 120 aminosyrer og findes ... SH3-domænet (efter Src homology 3) er et lille domæne af omkring 60 aminosyrer og findes i en række proteiner med forskellig ... The domains comprising each subunit of the phenylalanine hydroxylase *^ Structure and Interactions of NCAM Ig1-2-3 Suggest a ...
"The role of the Src homology 3-Src homology 2 interface in the regulation of Src kinases". J. Biol. Chem. 276 (20): 17199-205. ... "Regulation of the PH-domain-containing tyrosine kinase Etk by focal adhesion kinase through the FERM domain". Nat. Cell Biol. 3 ... 5-trisphosphate directs association of Src homology 2-containing signaling proteins with gelsolin". J. Biol. Chem. 276 (50): ... The C-terminal domain of FAK confers response to cell adhesion". J. Biol. Chem. 273 (4): 2384-9. PMID 9442086. doi:10.1074/jbc. ...
The N-terminus domain of LMP2A is tyrosine phosphorylated and associates with Src family protein tyrosine kinases (PTKs) as ... While the role of LMP2B in pathogenesis remains uncertain, homology studies comparing the LMP2 gene of EBV with Rhesus and ... These two iso forms of LMP2 only differ in that LMP2A contains an extra 119 residue N-terminal domain encoded in exon 1. ... LMP2B, unlike LMP2A, does not contain the N-terminal 119 amino acid cytoplasmic signaling domain. Most LMP2 research is focused ...
Gupta S, Davis RJ (October 1994). "MAP kinase binds to the NH2-terminal activation domain of c-Myc". FEBS Letters. 353 (3): 281 ... Upon cleavage, the C-terminus of Myc (containing the DNA binding domain) is degraded, while Myc-nick, the N-terminal segment ... Seth A, Alvarez E, Gupta S, Davis RJ (December 1991). "A phosphorylation site located in the NH2-terminal domain of c-Myc ... Myc-nick contains binding domains for histone acetyltransferases and for ubiquitin ligases. ...
This central region contains one src homology 3 (SH3) and two SH2 domains within a split PH domain, implying a series of ... Phospholipase C-γ Contains Introns Shared by src Homology 2 Domains in Many Unrelated Proteins. Charlene M. Manning, Wendy R. ... Phospholipase C-γ Contains Introns Shared by src Homology 2 Domains in Many Unrelated Proteins. Charlene M. Manning, Wendy R. ... Phospholipase C-γ Contains Introns Shared by src Homology 2 Domains in Many Unrelated Proteins. Charlene M. Manning, Wendy R. ...
Src homology 2 domain containing F is a protein that in humans is encoded by the SHF gene. GRCh38: Ensembl release 89: ... "Entrez Gene: Src homology 2 domain containing F". Retrieved 2018-05-27. CS1 maint: discouraged parameter (link) v t e. ...
Homologs of both the Src homology 2 and Src homology 3 domains are found in numerous other proteins. The Src homology 1 domain ... In biology, a Src homology domain is one of the two small protein binding domains found in the Src oncoprotein. ... In terms of initiating the cell cycle when growth factor signals are present, "Src homology domains" are found on Grb2 proteins ... was an early name of the protein kinase domain. ...
Defining the Specificity Space of the Human Src Homology 2 Domain. Haiming Huang, Lei Li, Chenggang Wu, David Schibli, Karen ... Defining the Specificity Space of the Human Src Homology 2 Domain. Haiming Huang, Lei Li, Chenggang Wu, David Schibli, Karen ... Defining the Specificity Space of the Human Src Homology 2 Domain. Haiming Huang, Lei Li, Chenggang Wu, David Schibli, Karen ... Defining the Specificity Space of the Human Src Homology 2 Domain Message Subject (Your Name) has sent you a message from ...
Deletion of Src homology 3 domain results in constitutive activation of Tec protein-tyrosine kinase.. Yamashita Y1, Miyazato A ... Deletion of the Src homology (SH) 3 domain gave rise to a hyperphosphorylated and activated Tec kinase (Tec deltaSH3). The ...
The C-terminal domain adopts a fold similar to eukaryotic Src homology 3 domains, but the functional role of the C-terminal ... and shown to be structurally homologous to eukaryotic Src homology 3 (SH3) domains, although the amino acid sequence homology ... Solution structure and peptide binding studies of the C-terminal Src homology 3-like domain of the diphtheria toxin repressor ... Solution structure and peptide binding studies of the C-terminal Src homology 3-like domain of the diphtheria toxin repressor ...
src homology 2;. SHP,. SH2-domain-containing protein tyrosine phosphatase;. KIR,. killer immunoglobulin-like receptor;. SHIP,. ... This tyrosine was phosphorylated and recruited src homology 2-domain-containing tyrosine phosphatase 2 (SHP-2) on coligation of ... PD-1 immunoreceptor inhibits B cell receptor-mediated signaling by recruiting src homology 2-domain-containing tyrosine ... PD-1 immunoreceptor inhibits B cell receptor-mediated signaling by recruiting src homology 2-domain-containing tyrosine ...
The C-terminal domain of bestrophins is proline rich and is predicted to contain src-homology (SH3)-binding domains (Hartzell ... The Best Disease-Linked Cl− Channel hBest1 Regulates CaV1 (L-type) Ca2+ Channels via src-Homology-Binding Domains. Kuai Yu, ... The Best Disease-Linked Cl− Channel hBest1 Regulates CaV1 (L-type) Ca2+ Channels via src-Homology-Binding Domains ... The Best Disease-Linked Cl− Channel hBest1 Regulates CaV1 (L-type) Ca2+ Channels via src-Homology-Binding Domains ...
1996) Distinct ligand preferences of src homology 3 domains from src, yes, abl, cortactin, p53bp2, PLCgamma, crk, and grb2. ... If the domain in the channel-kinase complex that interacts with the src SH3 motif peptide is an src-like SH3 domain, then a ... The most effective domain tested was the SH3 domain from src itself, which is part of one of the noncatalytic regions of the ... We also applied a mixture of 100 nm src SH3 domain plus 1 μm src SH3 motif peptide to excised patches and tested the effect on ...
The Src homology-2 (SH2) domains are modules of about 100 amino-acid residues that are found in many intracellular signal- ... The Src homology-2 (SH2) domains are modules of about 100 amino-acid residues that are found in many intracellular signal- ... Recognition of a high-affinity phosphotyrosyl peptide by the Src homology-2 domain of p56lck.. Eck, M.J., Shoelson, S.E., ... SH2 (SRC HOMOLOGY-2) DOMAIN OF HUMAN P56-LCK TYROSINE KINASE COMPLEXED WITH THE 11 RESIDUE PHOSPHOTYROSYL PEPTIDE EPQPYEEIPIYL ...
1 The abbreviations used are: PTK, protein-tyrosine kinase; SH2, Src homology 2; SH3, Src homology 3; EGF, epidermal growth ... Src Homology 2 Domain-based High Throughput Assays for Profiling Downstream Molecules in Receptor Tyrosine Kinase Pathways. ... Src Homology 2 Domain-based High Throughput Assays for Profiling Downstream Molecules in Receptor Tyrosine Kinase Pathways ... Src homology 2 (SH2) domains are evolutionary conserved small protein modules that bind specifically to tyrosine-phosphorylated ...
CD300F Blocks Both MyD88 and TRIF-Mediated TLR Signaling through Activation of Src Homology Region 2 Domain-Containing ... CD300F Blocks Both MyD88 and TRIF-Mediated TLR Signaling through Activation of Src Homology Region 2 Domain-Containing ... CD300F Blocks Both MyD88 and TRIF-Mediated TLR Signaling through Activation of Src Homology Region 2 Domain-Containing ... CD300F Blocks Both MyD88 and TRIF-Mediated TLR Signaling through Activation of Src Homology Region 2 Domain-Containing ...
Src homology region 2 domain-containing protein tyrosine phosphatase-1. shRNA. short hairpin RNA. SSG. sodium stibogluconate. ... The Src homology region 2 domain-containing tyrosine phosphatase-1 (SHP-1) is expressed in a wide variety of immune cells where ... We show that Src homology region 2 domain-containing phosphatase-1 (SHP-1) is an important inhibitor of DC signaling, targeting ... The Phosphatase Src Homology Region 2 Domain-Containing Phosphatase-1 Is an Intrinsic Central Regulator of Dendritic Cell ...
What is Src homology 2 domain-containing-transforming protein C4? Meaning of Src homology 2 domain-containing-transforming ... What does Src homology 2 domain-containing-transforming protein C4 mean? ... Src homology 2 domain-containing-transforming protein C4 explanation free. ... Looking for online definition of Src homology 2 domain-containing-transforming protein C4 in the Medical Dictionary? ...
Distribution of the Src-homology-2-domain-containing inositol 5-phosphatase SHIP-2 in both non-haemopoietic and haemopoietic ... Eric MURAILLE, Xavier PESESSE, Céline KUNTZ, Christophe ERNEUX; Distribution of the Src-homology-2-domain-containing inositol 5 ... The cDNA encoding a second SH2-domain-containing inositol 5-phosphatase, SHIP-2, has been cloned [Pesesse, Deleu, De Smedt, ... Numerous studies have demonstrated that the SH2-domain-containing inositol 5-phosphatase SHIP (referred hereto as SHIP-1) is ...
... domain and a C-terminal Src Homology 2 (SH2) domain. We show that SH2D5 is highly enriched in adult mouse brain, particularly ... Src homology 2 domain containing protein 5 (SH2D5) binds the breakpoint cluster region protein, BCR, and regulates levels of ... This interaction occurred between the PTB domain of SH2D5 and an NxxF motif located within the N-terminal region of BCR. siRNA- ... Despite harboring two potential phosphotyrosine (pTyr) recognition domains, SH2D5 binds minimally to pTyr ligands, consistent ...
In vitro and in cells the Src homology 3 (SH3) domain of DDEF2 and its close homolog, DDEF1, are associated with the SAMP motif ... Identification of a link between the SAMP repeats of adenomatous polyposis coli tumor suppressor and the Src homology 3 domain ... Our findings reveal that the SAMP motif of APC specifically binds to the SH3 domains of DDEFs, providing new insights into the ... NMR chemical shift perturbation experiments revealed that the SAMP motif interacts at the same surface of the SH3 domain of ...
src homology domain 3. TH1. tail homology domain 1. TH2. tail homology domain 2. YPD. rich, glucose-based media. ... Here, we report studies on the role of the tail homology domain 2 (TH2)1 and src homology domain 3 (SH3) domains of the Myo5p ... myo3Δ myo5Δ cells expressing mutant Myo5 proteins with deletions of the src homology domain 3 (SH3) or both TH2 and SH3 domains ... 1996) Yeast src homology 3 domain binding proteins involved in bud formation. J Cell Biol 133:865-878, pmid:8666671.. ...
... Lu ... The SH2-domain of Shb was found to bind to tyrosine 1175 in the VEGFR-2 in a phosphotyrosine dependent manner using PAE cells ... Medicine, Shb, Src, FAK, Angiogenesis, VEGFR-2, FGFR-1, Endothelial cells, Spreading, Stress fiber formation, siRNA, VEGF, FGF ... Uppsala University, Disciplinary Domain of Medicine and Pharmacy, Faculty of Medicine, Department of Medical Cell Biology. ...
Binding of Brutons tyrosine kinase to Fyn, Lyn, or Hck through a Src homology 3 domain-mediated interaction G Cheng, Z S Ye, D ... Here, we show that Btk interacts with Src homology 3 domains of Fyn, Lyn, and Hck, protein-tyrosine kinases that get activated ... Our data extend the range of interactions mediated by Src homology 3 domains and provide an indication of a link between Btk ... Binding of Brutons Tyrosine Kinase to Fyn, Lyn, or Hck Through a Src Homology 3 Domain-Mediated Interaction ...
Intracellular targeting, interaction with Src homology 3 (SH3) domains and rolipram-detected conformational switches in cAMP- ... Intracellular targeting, interaction with Src homology 3 (SH3) domains and rolipram-detected conformational switches in cAMP- ... Intracellular targeting, interaction with Src homology 3 (SH3) domains and rolipram-detected conformational switches in cAMP- ... Intracellular targeting, interaction with Src homology 3 (SH3) domains and rolipram-detected conformational switches in cAMP- ...
Targeting the Src Homology 2 (SH2) Domain of Signal Transducer and Activator of Transcription 6 (STAT6) with Cell-Permeable, ... Mandal, Pijus K., Morlacchi, Pietro, Knight, J. Morgan, et al.. "Targeting the Src Homology 2 (SH2) Domain of Signal Transducer ... We are developing phosphopeptide mimetics targeting the SH2 domain of STAT6 to block recruitment to phosphotyrosine residues on ... demonstrating that targeting the SH2 domain blocks both phosphorylation and transcriptional activity of STAT6. ...
Src family kinase; SH domain, Src homology domain; SPR, surface plasmon resonance. ... Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain. Sheraz ... Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain ... Activation of C-terminal Src kinase (Csk) by phosphorylation at serine-364 depends on the Csk-Src homology 3 domain ...
To study the role of the Src homology 2 (SH2) domain-containing protein Shb in angiogenesis, wild-type Shb and SH2 domain- ... Role of the Src Homology 2 Domain-containing Protein Shb in Murine Brain Endothelial Cell Proliferation and Differentiation1 ... The role of the Src Homology-2 domain containing protein B (SHB) in {beta} cells. J. Mol. Endocrinol., January 1, 2016; 56(1): ... Karlsson T., Welsh M. Apoptosis of NIH3T3 cells overexpressing the Src homology 2 domain protein Shb. Oncogene, 13: 955-961, ...
src Homology Domains abstract * Class IA PI3Ks are activated by growth factor receptors and generate lipid second messengers ... Inhibition of PI3K binding to activators by serine phosphorylation of PI3K regulatory subunit p85α Src homology-2 domains ... The p85 regulatory subunit of PI3K contains Src homology-2 (SH2) domains that mediate binding to tyrosine-phosphorylated ... The modified serine residues are located in the phospho-tyrosine binding pockets of the two SH2 domains, and in the crystal ...
... src Homology Domains/*immunology; src-Family Kinases/metabolism; Tumor Cells, Cultured/*immunology/metabolism; Type C ... Intracellular single-chain variable fragments directed to the Src homology 2 domains of Syk partially inhibit Fc epsilon RI ... Intracellular single-chain variable fragments directed to the Src homology 2 domains of Syk partially inhibit Fc epsilon RI ... directed against the portion of Syk containing the Src homology 2 domains and the linker region that separates them. Among them ...
Here, we show using wild-type and ship(-/-) osteoclasts that Src homology 2 (SH2)-containing 5-inositol phosphatase (SHIP) ... and this interaction appeared to be dependent on the Src kinase activity. These results demonstrate that c-Src enhances the ... SHIP was found to localize to podosomes under the influence of c-Src, and the presence of either the amino-terminal region ... Although SHIP lacking a functional SH2 domain was still found in podosomes, it could not rescue the hyper-bone resorbing ...
What is SHC (Src homology 2 domain containing) transforming protein 3? Meaning of SHC (Src homology 2 domain containing) ... What does SHC (Src homology 2 domain containing) transforming protein 3 mean? ... Src homology 2 domain containing) transforming protein 3 explanation free. ... Src homology 2 domain containing) transforming protein 3 in the Medical Dictionary? SHC ( ...
The SRC homology 2 domain protein Shep1 plays an important role in the penetration of olfactory sensory axons into the ... The SRC homology 2 domain protein Shep1 plays an important role in the penetration of olfactory sensory axons into the ... The SRC homology 2 domain protein Shep1 plays an important role in the penetration of olfactory sensory axons into the ...
... a C-terminal Src homology 2 (SH2) domain and an N-terminal phosphotyrosine-binding (PTB) domain, and is itself phosphorylated ... A mammalian adaptor protein with conserved Src homology 2 and phosphotyrosine-binding domains is related to Shc and is ... and an N-terminal PTB domain. The ShcC and ShcB SH2 domains bind phosphotyrosine-containing peptides and receptors with a ... The ShcC PTB domain specifically associates in vitro with the autophosphorylated receptors for nerve growth factor and ...
  • Homologs of both the Src homology 2 and Src homology 3 domains are found in numerous other proteins. (wikipedia.org)
  • In terms of initiating the cell cycle when growth factor signals are present, "Src homology domains" are found on Grb2 proteins, allowing them to bind Receptor Tyrosine Kinases (RTKs), and also on SOS proteins allowing them to interact with Grb2. (wikipedia.org)
  • SMALI interface for SH2 domain-binding ligand prediction ( A ) and its application to the prediction of Grb2 SH2-binding proteins ( B ). Only part of the predicted results is shown in the figure. (mcponline.org)
  • C , GST or GST-BRDG1 SH2 domain pulldown of endogenous proteins from A20 B cells. (mcponline.org)
  • SH3 and PDZ domains from other proteins were ineffective. (jneurosci.org)
  • The Src homology-2 (SH2) domains are modules of about 100 amino-acid residues that are found in many intracellular signal-transduction proteins. (rcsb.org)
  • More than 100 SH2 domains have been identified in proteins encoded by the human genome. (mcponline.org)
  • The binding specificity of these domains plays a critical role in signaling within the cell, mediating the relocalization and interaction of proteins in response to changes in tyrosine phosphorylation states. (mcponline.org)
  • We constructed 25-plex SH2 domain-GST fusion protein-conjugated fluorescent microsphere sets to investigate phosphorylation-mediated cell signaling through the specific binding of SH2 domains to activated target proteins. (mcponline.org)
  • Mutant Myo5 proteins with deletions in nonmotor domains were expressed in myo3Δ myo5Δ cells and the resulting strains were analyzed for Myo5p function. (rupress.org)
  • In contrast, myo3Δ myo5Δ cells expressing mutant Myo5 proteins with deletions of the src homology domain 3 (SH3) or both TH2 and SH3 domains display defects including Myo5p patch depolarization, actin disorganization, and phenotypes associated with actin dysfunction. (rupress.org)
  • Quite unexpectedly, we find that KorB-C shows a fold closely resembling the Src homology 3 (SH3) domain, a fold well known from proteins involved in eukaryotic signal transduction. (mdc-berlin.de)
  • Proline-rich sequences have been identified as binding sites for Src homology 3 (SH3) domains found in proteins associated with signal transduction events. (nih.gov)
  • The ability of these sequences to act as SH3 domain recognition motifs was investigated using bacterially expressed SH3 domains derived from several different signalling proteins. (nih.gov)
  • To assess the possible roles of cytokine-induced Src homology domain 2 (SH2) (CIS/SOCS) proteins in these transient responses, we studied the expression and disposition of CIS/SOCS proteins in rat adipocytes, a physiological target of GH action. (elsevier.com)
  • We named this protein Intersectin, because it potentially brings together EH and SH3 domain-binding proteins into a macromolecular complex. (elsevier.com)
  • Screens of a mouse embryo cDNA library with the EH domains of Intersectin yielded clones for the Rev-associated binding/Rev-interacting protein (RAB/Rip) and two novel proteins, which we named Intersectin-binding proteins (Ibps) 1 and 2. (elsevier.com)
  • Finally, affinity selection experiments with the SH3 domains of Intersectin identified two endocytic proteins, dynamin and synaptojanin, as potential interacting proteins. (elsevier.com)
  • The microtubule-associated protein tau can associate with various other proteins in addition to tubulin, including the SH3 domains of Src family tyrosine kinases. (edu.au)
  • Src homology (SH)2 and SH3 domains are found in a variety of proteins involved in the control of cellular signaling and architecture. (elsevier.com)
  • The Wiskott-Aldrich syndrome (WAS) family of proteins share similar domain structure, and are involved in transduction of signals from receptors on the cell surface to the actin cytoskeleton. (wikipedia.org)
  • The WASp family proteins includes WASp, N-WASp, SCAR/WAVE, WHAMM and WASH the five of them share a C- terminal VCA (verprolin, central, acidic) domain where they interact with actin nucleating complex (ARP2/3) and they differ in their terminal domains. (wikipedia.org)
  • In TNF-treated cells, TNFR1, TNFR-associated death domain protein (TRADD), Fas-associated death domain protein, and receptor-interacting protein kinase proteins form the signaling complex via modular interaction within their C-terminal death domains. (jimmunol.org)
  • Therefore, SXXE/D motifs found in the cytoplasmic domains of many TNFR family members and their adaptor proteins may serve to function as a specific interaction module for the α-helical death domain signal transduction. (jimmunol.org)
  • The C terminals of TNFR1, TRADD, FADD, and RIP all carry a discrete region termed the "death domain," which is composed of six continuous α-helical bundles and responsible for homotypic interactions among these four proteins. (jimmunol.org)
  • These are heterotrimeric G proteins, Src family kinases, and the recently cloned transmembrane adaptor protein linker for activation of T cells (LAT). (rupress.org)
  • Src family kinases and G proteins are anchored in the plasma membrane by means of NH 2 -terminal dual acylation with long saturated fatty acids ( 16 )( 17 ). (rupress.org)
  • Recent observations of bacterial proteins with putative phosphotyrosine binding pockets or Src homology 2 (SH2)-like domains suggest the presence of phosphotyrosine-dependent protein interaction networks. (asm.org)
  • Typical SH2B proteins contain a SH2 (Src homology 2) and a PH (pleckstrin homology) domain. (ebi.ac.uk)
  • There are 58927 SH2 domains in 53279 proteins in SMART's nrdb database. (embl-heidelberg.de)
  • Taxonomic distribution of proteins containing SH2 domain. (embl-heidelberg.de)
  • The complete taxonomic breakdown of all proteins with SH2 domain is also avaliable . (embl-heidelberg.de)
  • Click on the protein counts, or double click on taxonomic names to display all proteins containing SH2 domain in the selected taxonomic class. (embl-heidelberg.de)
  • The SH2 (Src Homology 2) domain is a structurally conserved protein domain contained within the Src oncoprotein and in many other intracellular signal-transducing proteins. (wikipedia.org)
  • SH2 domains allow proteins containing those domains to dock to phosphorylated tyrosine residues on other proteins. (wikipedia.org)
  • SH2 domains are commonly found in adaptor proteins that aid in the signal transduction of receptor tyrosine kinase pathways. (wikipedia.org)
  • A detailed bioinformatic examination of SH2 domains of human and mouse reveals 120 SH2 domains contained within 115 proteins encoded by the human genome, representing a rapid rate of evolutionary expansion among the SH2 domains. (wikipedia.org)
  • A large number of SH2 domain structures have been solved and many SH2 proteins have been knocked out in mice. (wikipedia.org)
  • The function of SH2 domains is to specifically recognize the phosphorylated state of tyrosine residues, thereby allowing SH2 domain-containing proteins to localize to tyrosine-phosphorylated sites. (wikipedia.org)
  • Tyrosine phosphorylation leads to activation of a cascade of protein-protein interactions whereby SH2 domain-containing proteins are recruited to tyrosine-phosphorylated sites. (wikipedia.org)
  • Using molecular biology techniques, fusion proteins of specific enzymes and SH2 domains have been created, which can bind to each other to form protein assemblies. (wikipedia.org)
  • The deduced protein of 368 aa contains a central α-helical region and a C-terminal Src homology 3 (SH3) domain most similar to the C-terminal SH3 domain found in the Grb2/Sem-5/Drk family of genes. (hku.hk)
  • The domain-swapped structure of Itk SH2 is similar to the domain-swapped SH2 domains of Grb2 and Nck, with domain swapping occurring at the β-meander region of all three SH2 domains. (iastate.edu)
  • In vitro binding assays indicate that four of these proline-rich sequences constitute specific binding sites for both SH3 domains of the adaptor molecule Grb2. (nih.gov)
  • We now report that tau can bind to SH3 domains derived from the p85α subunit of phosphatidylinositol 3-kinase, phospholipase Cγ1, and the N-terminal (but not the C-terminal) SH3 of Grb2 as well as to the kinases Fyn, cSrc, and Fgr. (edu.au)
  • abstract = "We report a novel series of non-peptide ligands that inhibit the growth factor receptor-bound protein 2 (Grb2)-Src homology 2 (SH2) domain binding, designed using a combined computational and NMR-driven approach. (uab.cat)
  • Thus, 1n can be used as a scaffold for the development of efficient Grb2-SH2 domain binding inhibitors. (uab.cat)
  • Recent crystallographically derived structures of the Src SH2 domain in complex with low-affinity peptides, which do not contain the EEI consensus, and NMR-derived structures of unliganded Abl (ref. 19) and p85 (ref. 20) SH2 domains have revealed the conserved fold of the SH2 domain and the properties of a phosphotyrosine binding pocket. (rcsb.org)
  • SH2D5 is a mammalian-specific, uncharacterized adaptor-like protein that contains an N-terminal phosphotyrosine binding (PTB) domain and a C-terminal Src Homology 2 (SH2) domain. (mdc-berlin.de)
  • Despite harboring two potential phosphotyrosine (pTyr) recognition domains, SH2D5 binds minimally to pTyr ligands, consistent with the absence of a conserved pTyr-binding arginine residue in the SH2 domain. (mdc-berlin.de)
  • FGF stimulation led to a direct association between Shb and FAK, which was mediated by the phosphotyrosine binding domain of Shb. (diva-portal.org)
  • The SH2-domain of Shb was found to bind to tyrosine 1175 in the VEGFR-2 in a phosphotyrosine dependent manner using PAE cells expressing VEGFR-2. (diva-portal.org)
  • We are developing phosphopeptide mimetics targeting the SH2 domain of STAT6 to block recruitment to phosphotyrosine residues on IL-4 or IL-13 receptors and subsequent Tyr641 phosphorylation to inhibit the expression of genes contributing to asthma. (rice.edu)
  • Src homology 2 domains bind phosphotyrosine-containing polypeptides via 2 surface pockets. (embl-heidelberg.de)
  • Here, we show that Btk interacts with Src homology 3 domains of Fyn, Lyn, and Hck, protein-tyrosine kinases that get activated upon stimulation of B- and T-cell receptors. (caltech.edu)
  • PAG comprises a short extracellular domain of 16 amino acids and a 397-amino acid cytoplasmic tail containing ten tyrosine residues that are likely phosphorylated by Src family kinases. (rupress.org)
  • In lymphoid cell lines and in resting peripheral blood α/β T cells, PAG is expressed as a constitutively tyrosine-phosphorylated protein and binds the major negative regulator of Src kinases, the tyrosine kinase Csk. (rupress.org)
  • Signal transduction by immunoreceptors (TCRs, B cell receptors, and most Fc receptors) after their aggregation by natural ligands or Abs is initiated by activation of protein tyrosine kinases (PTKs) of the Src and Syk families, which phosphorylate a variety of substrates, thus allowing propagation of the initial stimulus to cytosolic signaling pathways ( 1 ). (rupress.org)
  • In tumor cells, constitutive activation of STATs is linked to persistent activity of tyrosine kinases, including Src, epidermal growth factor receptor, Janus kinases, Bcr-Abl, and many others. (aacrjournals.org)
  • and Src family tyrosine kinases. (bloodjournal.org)
  • BY-kinases have two transmembrane domains and typical Walker A and B ATP binding motifs in their cytoplasmic catalytic domain. (asm.org)
  • Growth factor receptor-binding protein 10 (Grb10) is a pleckstrin homology and Src homology 2 (SH2) domain-containing protein that interacts with several receptor tyrosine kinases, including the insulin receptor (IR) and the IGF-1 receptor (IGF1R) ( 5 , 6 ). (diabetesjournals.org)
  • In this way, phosphorylation of a substrate by tyrosine kinases acts as a switch to trigger binding to an SH2 domain-containing protein. (wikipedia.org)
  • The intimate relationship between tyrosine kinases and SH2 domains is supported by their coordinate emergence during eukaryotic evolution. (wikipedia.org)
  • This tyrosine was phosphorylated and recruited src homology 2-domain-containing tyrosine phosphatase 2 (SHP-2) on coligation of PD-1 with BCR. (pnas.org)
  • Use of specific inhibitors and immunoprecipitation analysis further indicated that the inhibitory effects were mediated by Src homology 2 domain-containing phosphatase-1, a protein tyrosine phosphatase with inhibitory activity in hematopoietic cells. (jimmunol.org)
  • These data indicate that CD300F is an active regulator of TLR-mediated macrophage activation through its association with Src homology 2 domain-containing phosphatase-1 and that the synthetic peptides can be applied for the regulation of immune responses that are induced by TLRs. (jimmunol.org)
  • We show that Src homology region 2 domain-containing phosphatase-1 (SHP-1) is an important inhibitor of DC signaling, targeting multiple activation pathways. (jimmunol.org)
  • The Src homology region 2 domain-containing tyrosine phosphatase-1 (SHP-1) is expressed in a wide variety of immune cells where it plays a largely inhibitory role in cell signaling initiated through a range of cytokine, chemokine, growth factor, and AgR stimuli ( 7 ). (jimmunol.org)
  • Numerous studies have demonstrated that the SH2-domain-containing inositol 5-phosphatase SHIP (referred hereto as SHIP-1) is essential in this process. (portlandpress.com)
  • The cDNA encoding a second SH2-domain-containing inositol 5-phosphatase, SHIP-2, has been cloned [Pesesse, Deleu, De Smedt, Drayer and Erneux (1997) Biochem. (portlandpress.com)
  • Src homology 2 (SH2)-containing 5'-inositol phosphatase localizes to podosomes, and the SH2 domain is implicated in the attenuation of bone resorption in osteoclasts. (semanticscholar.org)
  • Here, we show using wild-type and ship(-/-) osteoclasts that Src homology 2 (SH2)-containing 5'-inositol phosphatase (SHIP) appeared to negatively regulate bone resorption activated by c-Src. (semanticscholar.org)
  • Together, these results describe a novel SH3 domain-dependent recruitment of a protein tyrosine phosphatase to an activated receptor tyrosine kinase and establish a potential role for MPTP-PEST in signalling pathways at the molecular level. (nih.gov)
  • Expression of src homology domain 2 (SH2)-containing tyrosine phosphatase-1 (SHP-1), phosphorylated Janus kinase 2 (p-JAK2), and phosphorylated signal transducer and activator of transcription 5 (p-STAT5) was assessed with Western blot analysis. (elsevier.com)
  • In view of the role for the Src homology domain 2-bearing protein tyrosine phosphatase- 1 (SHP-1) in modulating TCR signaling, we investigated the influence of SHP- 1 on TCR-mediated apoptosis by assaying the sensitivity of peripheral T cells from SHP-1-deficient viable motheaten (me(v)) mice to cell death following TCR restimulation. (elsevier.com)
  • Since SH2 domains require phosphorylation in order for binding to occur, the use of kinase and phosphatase enzymes gives researchers control over whether protein assemblies will form or not. (wikipedia.org)
  • Kay, Brian K. / Intersectin, a novel adaptor protein with two Eps15 homology and five Src homology 3 domains . (elsevier.com)
  • TNF-bound TNFR1 recruits TNFR-associated death domain protein (TRADD), an adaptor protein that serves as the platform for additional recruitment of receptor-interacting protein kinase (RIP) and Fas-associated death domain protein (FADD), initiating both NF-κB activation and apoptosis induction ( 1 - 3 ). (jimmunol.org)
  • Grb10 negatively regulates insulin or IGF-1 signaling by binding to the kinase domain of the tyrosine-phosphorylated IR or IGF1R, mainly via its SH2 domain and partly a region between the pleckstrin homology domain and the SH2 domain (BPS) ( 9 , 12 - 14 ). (diabetesjournals.org)
  • PAPbeta, a protein that binds to and is phosphorylated by the non-receptor tyrosine kinase PYK2, contains several modular signaling domains including a pleckstrin homology domain, an SH3 domain, ankyrin repeats and an ARF-GAP domain. (embl-heidelberg.de)
  • The solution structure of the C-terminal domain, consisting of residues N130-L226 plus a 13-residue N-terminal extension, has been determined by using NMR spectroscopy. (pnas.org)
  • Residues before A147 are highly mobile and adopt a random coil conformation, but residues A147-L226 form a single structured domain consisting of five β-strands and three helices arranged into a partially orthogonal, two-sheet β-barrel, similar to the structure observed in the crystalline Co 2+ complex of full-length DtxR. (pnas.org)
  • Chemical shift perturbation studies demonstrate that a proline-rich peptide corresponding to residues R125-G139 of intact DtxR binds to the C-terminal domain in a pocket formed by residues in β-strands 2, 3, and 5, and helix 3. (pnas.org)
  • From the sequential assignment of resonances in heteronuclear NMR spectra of a recombinant C-terminal domain (residues N130-L226), we have shown that this isolated domain contains five β-strands and three helices ( 14 ). (pnas.org)
  • NMR chemical shift perturbation studies demonstrate that a synthetic peptide corresponding to this internal ligand interacts with specific amino acid residues in the C-terminal domain. (pnas.org)
  • On stimulation, tyrosine residues of ITIMs are usually phosphorylated to recruit Src homology 2 (SH2)-containing phosphatases that play critical roles in negative regulation of cellular activities. (pnas.org)
  • In the low-affinity phosphopeptide/Src complexes, the pY + 3 residues do not insert into the homologous binding pocket and the peptide main chain remains displaced from the surface of the domain. (rcsb.org)
  • Here we report the crystal structure of KorB-C, the C-terminal domain of KorB comprising residues 297-358. (mdc-berlin.de)
  • Binding of cytokines to their receptors triggers a conformational change of usually pre-formed dimers [ 7 , 8 ] that are transmitted to the cytosolic domains, which leads to cross-phosphorylation and activation of JAKs that phosphorylate tyrosine residues on the cytosolic domains of receptors. (biochemsoctrans.org)
  • The SH2 domain, which was first identified in the oncoproteins Src and Fps, is about 100 amino-acid residues long. (wikipedia.org)
  • Here we developed an SH2 domain profiling method based on a multiplexed fluorescent microsphere assay in which various SH2 domains are used to probe the global state of tyrosine phosphorylation within a cell and to screen synthetic peptides that specifically bind to each SH2 domain. (mcponline.org)
  • IL-13-stimulated expression of CCL26 (eotaxin-3) was inhibited in a dose-dependent manner, demonstrating that targeting the SH2 domain blocks both phosphorylation and transcriptional activity of STAT6. (rice.edu)
  • Furthermore, the interaction between the SH3 and kinase domains was facilitated by PKA-mediated phosphorylation of the kinase domain, as evaluated by surface plasmon resonance. (biochemj.org)
  • ArgBP2 contains three COOH-terminal Src homology 3 domains, a serine/threonine-rich domain, and several potential Abl phosphorylation sites. (semanticscholar.org)
  • These compounds showed high-affinity binding to Stat3's SH2 domain, inhibited intracellular Stat3 phosphorylation, and induced apoptosis in MM cell lines at low micromolar concentrations. (ox.ac.uk)
  • Expression of PAG in COS cells results in recruitment of endogenous Csk, altered Src kinase activity, and impaired phosphorylation of Src-specific substrates. (rupress.org)
  • The N-terminal SH2 domains of cytoplasmic tyrosine kinase was at the beginning of evolution evolved with the occurrence of tyrosine phosphorylation. (wikipedia.org)
  • We also present evidence that this prokaryotic SH3-like domain binds to a proline-rich segment that is located in the region linking the N- and C-terminal domains of DtxR and is conserved in all known DtxR homologues. (pnas.org)
  • Modulation was also prevented by an SH3 motif peptide that preferentially binds the SH3 domain of src. (jneurosci.org)
  • Our findings reveal that the SAMP motif of APC specifically binds to the SH3 domains of DDEFs, providing new insights into the functions of APC in cell migration. (nih.gov)
  • The proline-rich protein verprolin (Vrp1p) binds to the SH3 domain of Myo3p or Myo5p in two-hybrid tests, coimmunoprecipitates with Myo5p, and colocalizes with Myo5p. (rupress.org)
  • We have previously shown that after T-cell antigen receptor stimulation, Lck binds to ZAP-70 via its Src homology 2 (SH2) domain (LckSH2) and, more recently, that Tyr319 of ZAP-70 is phosphorylated in vivo and plays a positive regulatory role. (ox.ac.uk)
  • This exposes a domain near the WASp C-terminus that binds to and activates the Arp2/3 complex . (wikipedia.org)
  • The SH2 domain preferentially binds phosphopeptides with the consensus sequence Y-[TVI]-X-L and mediates interaction with PDGFRA, PDGFRB, FGRFR1, IL2RB, IL2RG, CD3Z and CRK/CrKII. (abcam.com)
  • The KLERQ domain binds to SNAP-25 and SNAP-23. (abcam.com)
  • To determine whether the association between the kinase and the cation channel involves specific forms of protein-protein interactions, we have tested the ability of different interaction domains and motifs to interfere with the functional link between channel and kinase in excised, inside-out patches. (jneurosci.org)
  • In this paper, we report that the death domain SXXE/D motifs (i.e. (jimmunol.org)
  • S381DHE motif of TNFR1-death domain as well as S215LKD and S296LAE motifs of TRADD-death domain) are phosphorylated, and this is required for stable TNFR1-TRADD complex formation and subsequent activation of NF-κB. (jimmunol.org)
  • Phospho-S215LKD and phospho-S296LAE motifs are also critical to TRADD for recruiting Fas-associated death domain protein and receptor-interacting protein kinase. (jimmunol.org)
  • Many tyrosine containing short linear motifs that bind to SH2 domains are conserved across a wide variety of higher Eukaryotes. (wikipedia.org)
  • Disruption of FAK function by overexpression of the FAK C-terminal domain [FAK-CD, analogous to the FRNK (FAK-related non-kinase) protein] leads to loss of adhesion and apoptosis in tumour cells. (portlandpress.com)
  • each domain is presumed to have arisen once and then been spread both by gene duplication and by being co-opted into existing genes by exon shuffling via retrotransposition, illegitimate recombination, or long interspersed nuclear element-mediated 3′ transduction ( L ong 2001 ). (genetics.org)
  • SHE (Src Homology 2 Domain Containing E) is a Protein Coding gene. (genecards.org)
  • We have also used whole-cell recording to introduce interaction domains into bag cell neurons and observe their effects on cation channel-induced depolarization. (jneurosci.org)
  • Our data indicate that the cation channel-kinase "association" requires src homology 3 (SH3) domain protein-protein interactions, and that disruption of this interaction prevents channel modulation and attenuates the long-lasting depolarization produced by cation channel activation. (jneurosci.org)
  • This interaction occurred between the PTB domain of SH2D5 and an NxxF motif located within the N-terminal region of BCR. (mdc-berlin.de)
  • This suggests that an overall structural domain organization and interaction between the kinase and SH3 domains are important for the activity of Csk and its regulation by PKA. (biochemj.org)
  • Interaction of the FLT3 receptor with FL causes receptor dimerization, leading to the activation of its tyrosine kinase domain and receptor autophosphorylation. (bloodjournal.org)
  • Furthermore, Shb-induced cell spreading on collagen of immortalised brain endothelial (IBE) cells was also Src-dependent. (diva-portal.org)
  • IBE cells overexpressing wild-type or R522K Shb (inactive SH2 domain) displayed increased FAK activation on collagen. (diva-portal.org)
  • Upon binding to its ligand, IGF-IR undergoes autophosphorylation and conformational changes that trigger an intracellular signaling cascade through the insulin receptor substrates 1 to 4 (IRS1-IRS4) and Src homology and collagen. (aacrjournals.org)
  • A circle denotes that an OPAL-derived motif is available for that SH2 domain. (mcponline.org)
  • No binding motif has been described for subgroup IE SH2 domains. (mcponline.org)
  • In vitro and in cells the Src homology 3 (SH3) domain of DDEF2 and its close homolog, DDEF1, are associated with the SAMP motif of APC competitively with Axin1. (nih.gov)
  • Moreover, NMR chemical shift perturbation experiments revealed that the SAMP motif interacts at the same surface of the SH3 domain of DDEF as the known SH3 binding motif, PXXP. (nih.gov)
  • Several experiments support the conclusion that the free carboxylate group contributes to binding of the NPFL motif at the C terminus of RAB/Rip to the EH domains of Intersectin. (elsevier.com)
  • Sequences of ARF-GAP domains show no recognizable similarity to those of other GAPs, and contain a characteristic Cys-X(2)-Cys-X(16-17)-Cys-X(2)-Cys motif. (embl-heidelberg.de)
  • The ARF-GAP domain comprises a central three-stranded beta-sheet flanked by five alpha-helices, with a Zn(2+) ion coordinated by the four cysteines of the cysteine-rich motif. (embl-heidelberg.de)
  • SH2 domains typically bind a phosphorylated tyrosine residue in the context of a longer peptide motif within a target protein, and SH2 domains represent the largest class of known pTyr-recognition domains. (wikipedia.org)
  • Deletion of Src homology 3 domain results in constitutive activation of Tec protein-tyrosine kinase. (nih.gov)
  • Furthermore, whole-cell depolarizations elicited by cation channel activation were decreased by the src SH3 domain. (jneurosci.org)
  • In the present study, we investigate the mechanism for the protein kinase A (PKA)-mediated activation of C-terminal Src kinase (Csk). (biochemj.org)
  • Although isolated Csk kinase domain was phosphorylated at Ser 364 by PKA to the same stoichiometry as wild-type Csk, significant activation of the isolated Csk kinase domain by PKA was observed only in the presence of the purified Src homology 3 domain (SH3 domain). (biochemj.org)
  • Collectively, our findings indicate that Tyr319-mediated binding of the SH2 domain of Lck is crucial for ZAP-70 activation and consequently for the propagation of the signaling cascade leading to T-cell activation. (ox.ac.uk)
  • Inhibiting aberrant signal transducer and activator of transcription protein activation with tetrapodal, small molecule Src homology 2 domain binders: promising agents against multiple myeloma. (ox.ac.uk)
  • 30 , 31 Somatic mutations of FLT3 involving in-frame internal tandem duplications (ITDs) in the juxtamembrane domain or D835 point mutations in the activation loop occur in 17% to 34% and 7% of patients with AML, respectively. (bloodjournal.org)
  • Determination of SH2 domain specificity by OPAL screen. (mcponline.org)
  • Within each major class, the SH2 domains are further divided into subgroups based on binding specificity from the OPAL screens and the literature. (mcponline.org)
  • The C-terminal domain adopts a fold similar to eukaryotic Src homology 3 domains, but the functional role of the C-terminal domain in repressor activity is unknown. (pnas.org)
  • The structure of the C-terminal 90 aa, which is more mobile than the N-terminal domain in all crystal forms, has been mapped in the Co 2+ -DtxR complex ( 9 ) and shown to be structurally homologous to eukaryotic Src homology 3 (SH3) domains, although the amino acid sequence homology is low. (pnas.org)
  • The N-terminal domain is structurally well-defined and is responsible for Fe 2+ binding, dimerization, and DNA binding. (pnas.org)
  • The possible interrelationships between domains are not easily investigated, even though several cases of multiple domain-containing constructs have been studied structurally. (elsevier.com)
  • A pleckstrin homology-related domain in SHIP1 mediates membrane localization during Fcγ receptor-induced phagocytosis. (semanticscholar.org)
  • Results: The Src homology 3 domain-containing GEF (SGEF) promotes fibroblast growth factor-inducible 14 (Fn14) proinvasive signaling in glioblastoma via TNF receptor-associated factor 2 (TRAF2). (elsevier.com)
  • Interacts with phosphorylated Tyr-720 of PDGFRA via its SH2 domain. (genecards.org)
  • [9] WASp interacting protein (WIP) interacts with WASp N-terminal domain (WH1) preventing it from degradation and stabilising its auto-inhibitory conformation. (wikipedia.org)
  • A , correlation of SMALI score with dissociation free energy for peptides predicted to bind the SH2D1A SH2 domain. (mcponline.org)
  • B , correlation of free energy with SMALI scores for peptides predicted to bind the BRDG1 SH2 domain based on data shown in Table II. (mcponline.org)
  • Src homology 2 (SH2) domains are evolutionary conserved small protein modules that bind specifically to tyrosine-phosphorylated peptides. (mcponline.org)
  • Two of these types were shown to bind to both SH2 and SH3 dual domains with high affinities and specificities, showing increases of one order of magnitude, as compared to the most strongly bound monovalent equivalent. (elsevier.com)
  • SH3-3, SH3-4 and SH3-5, but not SH3-1 and SH3-2 domains, bind to dynamin (By similarity). (abcam.com)
  • The domains are frequently found as repeats in a single protein sequence and will then often bind both mono- and di-phosphorylated substrates. (embl-heidelberg.de)
  • Consolidated ligands combine in the same molecule peptide sequences recognized by SH2 and SH3 domains, i.e. (elsevier.com)
  • SMALI prediction and validation of SH2 domain-ligand interactions. (mcponline.org)
  • These data suggest that the cation channel-PKC association may require SH3 domain-mediated interactions to bring about modulation, promote membrane depolarization, and initiate prolonged changes in bag cell neuron excitability. (jneurosci.org)
  • Our data extend the range of interactions mediated by Src homology 3 domains and provide an indication of a link between Btk and established signaling pathways in B lymphocytes. (caltech.edu)
  • The KorB-C crystal structure extends the range of protein-protein interactions known to be promoted by SH3 and SH3-like domains. (mdc-berlin.de)
  • Modular domains, which are the subunits of a protein, moderate these protein interactions by identifying short peptide sequences. (wikipedia.org)
  • Other applications of SH2 domain mediated protein assemblies have been in the formation of high density fractal-like structures, which have extensive molecular trapping properties. (wikipedia.org)
  • To investigate the effect of CD300F stimulation on TLR signaling, the human acute monocytic leukemia cell line THP-1 was treated with CD300F-specific mAbs or two synthetic peptides that represented the ITIM-like domains of CD300F. (jimmunol.org)
  • The experimentally determined binding of tau peptides is well accounted for when modeled into the peptide binding cleft in the SH3 domain of Fyn. (edu.au)
  • We screened a Xenopus laevis oocyte cDNA expression library with a Src homology 3 (SH3) class II peptide ligand and identified a 1270-amino acid- long protein containing two Eps15 homology (EH) domains, a central coiled- coil region, and five SH3 domains. (elsevier.com)
  • A limited number of mutations in the C-terminal domain ( 12 ) or the linker region ( 13 ) affect repressor activity, but the structural nature of this regulation by the C-terminal domain has been obscure. (pnas.org)
  • The discovery of the highly prevalent activating JAK (Janus kinase) 2 V617F mutation in myeloproliferative neoplasms, and of other pseudokinase domain-activating mutations in JAK2, JAK1 and JAK3 in blood cancers, prompted great interest in understanding how pseudokinase domains regulate kinase domains in JAKs. (biochemsoctrans.org)
  • Mutations were found in exons 21 and 20, encoding the Src homology 2 domain. (uptodate.com)
  • The region of hBest1 responsible for the effect was localized to a region (amino acids 330-370) in the cytoplasmic C terminus that contains a predicted src-homology-binding domain that is not present in other bestrophin subtypes. (jneurosci.org)
  • Immunolocalization of the myc-tagged SH3 domain of Myo5p reveals diffuse cytoplasmic staining. (rupress.org)
  • Comparison of intron positions demonstrates that extensive intron loss has occurred during invertebrate evolution and also reveals the presence of conserved introns in both the N- and C-terminal PLC-γ SH2 domains that are present in SH2 domains in many other genes. (genetics.org)
  • These and other conserved SH2 introns suggest that the SH2 domains in PLC-γ are derived from an ancestral domain that was shuffled not only into PLC-γ, but also into many other unrelated genes during animal evolution. (genetics.org)
  • In biology, a Src homology domain is one of the two small protein binding domains found in the Src oncoprotein. (wikipedia.org)
  • Crystal structures of vertebrate PTP domains show conserved fold and consistent Cα-backbone trace. (asm.org)
  • Deletion of the Src homology (SH) 3 domain gave rise to a hyperphosphorylated and activated Tec kinase (Tec deltaSH3). (nih.gov)
  • Deletion of the tail homology 2 (TH2) domain, previously implicated in ATP-insensitive actin binding, has no detectable effect on Myo5p function. (rupress.org)
  • Deletion of the C-terminal sequence, NPFL-COOH, from RAB/Rip eliminated EH domain binding, whereas fusion of the same peptide sequence to glutathione S-transferase generated strong binding to the EH domains of Intersectin. (elsevier.com)
  • PTPs having closely related catalytic domains also tend to be similar in overall structural topology. (asm.org)
  • PLC-γ is particularly interesting from an evolutionary standpoint, because it has a central region between the X and Y catalytic domains that is unique among PLC subtypes. (genetics.org)
  • This central region contains one src homology 3 (SH3) and two SH2 domains within a split PH domain, implying a series of shufflings and duplications to produce the modern PLC-γ structure from an ancestral PLC form. (genetics.org)
  • We isolated from a phage display library human single-chain variable fragments (scFv) directed against the portion of Syk containing the Src homology 2 domains and the linker region that separates them. (cnrs.fr)
  • SHIP was found to localize to podosomes under the influence of c-Src, and the presence of either the amino-terminal region comprising the SH2 domain or the carboxyl-terminal region was sufficient for its localization. (semanticscholar.org)
  • The output region is called the VVCA domain. (wikipedia.org)
  • However, in full-length N-WASp the control region suppresses VCA domain activity. (wikipedia.org)
  • [9] The control region contains a CDC42-binding domain (GBP) and a PIP2-binding domain (B), both of which are critical for proper regulation of N-WASp. (wikipedia.org)
  • Our results suggest a model in which Src regulates adhesion and survival through enhanced expression of the α2-integrin. (portlandpress.com)
  • A phosphopeptide library screen has recently been used to deduce an 'optimal' binding sequence for the Lck SH2 domain. (rcsb.org)
  • Sequence analysis of the fusion MLL/EEN transcript in our patient reveals that exon 6 of MLL is fused to the N- terminal end of EEN, a fusion that would create a chimeric protein that includes the major functional domain of EEN. (hku.hk)
  • The detailed analysis of the dimer interface and a chemical cross-linking study suggest that the C-terminal domain is responsible for stabilizing the dimeric form of KorB in solution to facilitate binding to the palindromic operator sequence. (mdc-berlin.de)
  • Sequence comparison of human PTP domains. (asm.org)
  • Shown is an amino acid sequence alignment of 37 human PTP domains (from nontransmembrane PTP and RPTP domains D1) (above) and comparison with domain D2 sequences of RPTPs (below). (asm.org)
  • Determination of sequence similarity among PTP catalytic domains (Fig. 2 ) was used to classify the PTP family of enzymes into nine nontransmembrane PTP subtypes (NT) and eight RPTP subtypes (R). Only the human PTPs are listed, and a representative member of each subtype is shown. (asm.org)
  • D , isothermal binding curves to the BRDG1 SH2 domain for an NTAL-derived phosphopeptide and a Leu(P + 4) to Ala analog. (mcponline.org)
  • We report here the high-resolution crystallographic analysis of the Lck SH2 domain in complex with this phosphopeptide. (rcsb.org)
  • This peptide is docked to the SH2 domains of Fes and HSH2D in C and D , respectively, based on structural superposition. (mcponline.org)
  • Binding of the proline-rich peptide by the C-terminal domain of DtxR presents an example of peptide binding by a prokaryotic Src homology 3-like protein. (pnas.org)
  • The demonstration of peptide binding by the C-terminal domain suggests a possible mechanism for regulating the activity of the intact repressor protein. (pnas.org)
  • The ligand preference of the EH domains were deduced to be asparajine-proline-phenylalanine (NPF) or cyclized NPF (CX(1- 2)NPFXXC), depending on the type of phage-displayed combinatorial peptide library used. (elsevier.com)
  • We have also shown that expression of activated Src in breast cancer cells increased the expression of α2-integrin and that overexpression of α2-integrin suppressed FAK-CD-mediated loss of adhesion. (portlandpress.com)
  • The Src homology 1 domain was an early name of the protein kinase domain. (wikipedia.org)
  • JAK2, via its FERM domain, promotes cell-surface localization and stabilization of cytokine receptors, such as EpoR and TpoR. (biochemsoctrans.org)