Properties of the src kinase purified from Rous sarcoma virus-induced rat tumors.
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Analysis of the products of the phosphorylation reaction by thin layer chromatography revealed that the src kinase phosphorylates glycerol in addition to casein or the enzyme itself, indicating that the enzyme is very sensitive to increased ionic strength.About:
This article is published in Journal of Biological Chemistry.The article was published on 1982-06-25 and is currently open access. It has received 95 citations till now. The article focuses on the topics: Casein kinase 2, alpha 1 & Enzyme assay.read more
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Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins.
TL;DR: Addition of vanadate to the culture medium of NRK-1 cells resulted in a maximal 40-fold increase in the level of phosphotyrosine in cell protein and induced transformation as evidenced by four criteria: generation of a highly refractile morphology, decreased density-dependent growth inhibition, increased rates of uptake of 2-deoxyglucose, and growth in the absence of a solid support.
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Down-regulation of the Filamentous Actin Cross-linking Activity of Cortactin by Src-mediated Tyrosine Phosphorylation
TL;DR: This study presents the first evidence that pp60c-src can directly regulate the activity of its substrate toward the cytoskeleton and implies a role of cortactin as an F-actin modulator in tyrosine kinase-regulated cytoskeletal reorganization.
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Analysis of pp60c-src protein kinase activity in human tumor cell lines and tissues.
TL;DR: Observations suggest that increases in the specific activity of the pp60c-src phosphotransferase in some rhabdomyosarcomas and breast carcinomas may be a characteristic acquired during the malignant transformation of the cells that is retained in cell lines established from these tumors.
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Synthetic tyrosine polymers as substrates and inhibitors of tyrosine-specific protein kinases.
TL;DR: Several synthetic random polymers of tyrosine containing glutamic acid, alanine, and lysine in various proportion served as substrates for tyrosin-specific protein kinases, and several synthetic polymers with ordered sequences were found to be potent inhibitors of these tyosine-specificprotein kinases.
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Dephosphorylation or antibody binding to the carboxy terminus stimulates pp60c-src.
J A Cooper,C S King +1 more
TL;DR: It is suggested that the phosphorylated carboxy terminus acts as an inhibitor of the protein kinase domain of pp60c-src, unless its conformation is altered by either dephosphorylation or antibody binding, which suggests that other protein-tyrosine kinases may normally phosphorylate Tyr-527 and regulate pp60C-src in the cell.
References
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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
TL;DR: Using an improved method of gel electrophoresis, many hitherto unknown proteins have been found in bacteriophage T4 and some of these have been identified with specific gene products.
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Transforming gene product of Rous sarcoma virus phosphorylates tyrosine
TL;DR: It is inferred that pp60src is a novel protein kinase and that the modification of proteins via the phosphorylation of tyrosine is essential to the malignant transformation of cells by Rous sarcoma virus.
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Protein kinase activity associated with the avian sarcoma virus src gene product.
TL;DR: The expression of the protein kinase activity (ATP:protein phosphotransferase, EC 2.7.1.37) was growth temperature-dependent in cells infected with an ASV mutant temperature-sensitive for the transformation, and this activity was discussed in terms of protein phosphorylation as a mechanism for viral transformation.
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Identification of a transformation-specific antigen induced by an avian sarcoma virus.
TL;DR: The identification of a 60,000-MW transformation-specific antigen detectable in ASV-transformed chicken cells andASV-induced hamster tumour cells is described by immunoprecipitation of radiolabelled cell extracts with serum from tumour-bearing rabbits.
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Evidence that the transforming gene of avian sarcoma virus encodes a protein kinase associated with a phosphoprotein.
TL;DR: It is concluded that both the protein kinase and pp60 are encoded in src, and that the enzymatic activity may be an intrinsic property of pp60.