pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions
Autor: | R R Vines, C A Borgman, J T Parsons, Albert B. Reynolds, Michael D. Schaller, B S Cobb |
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Rok vydání: | 1992 |
Předmět: |
animal structures
Molecular Sequence Data Restriction Mapping PTK2 Fluorescent Antibody Technique Chick Embryo Biology Mitogen-activated protein kinase kinase SH3 domain MAP2K7 chemistry.chemical_compound Tensins Cell Adhesion Animals Amino Acid Sequence Cloning Molecular Multidisciplinary Base Sequence Microfilament Proteins Tyrosine phosphorylation DNA Protein-Tyrosine Kinases Focal Adhesion Kinase 2 Cell Transformation Viral Phosphoproteins Molecular biology Molecular Weight Cytoskeletal Proteins chemistry Focal Adhesion Kinase 1 Focal Adhesion Protein-Tyrosine Kinases Cyclin-dependent kinase 9 Cell Adhesion Molecules Sequence Alignment Research Article Proto-oncogene tyrosine-protein kinase Src |
Zdroj: | Proceedings of the National Academy of Sciences. 89:5192-5196 |
ISSN: | 1091-6490 0027-8424 |
DOI: | 10.1073/pnas.89.11.5192 |
Popis: | Expression of the Rous sarcoma virus-encoded oncoprotein, pp60v-src, subverts the normal regulation of cell growth, which results in oncogenic transformation. This process requires the intrinsic protein-tyrosine kinase activity of pp60v-src and is associated with an increase in tyrosine phosphorylation of a number of cellular proteins, candidate substrates for pp60v-src. We report here the isolation of a cDNA encoding a protein, pp125, that is a major phosphotyrosine-containing protein in untransformed chicken embryo cells and exhibits an increase in phosphotyrosine in pp60v-src-transformed chicken embryo cells. This cDNA encodes a cytoplasmic protein-tyrosine kinase which, based upon its predicted amino acid sequence and structure, is the prototype for an additional family of protein-tyrosine kinases. Immunofluorescence localization experiments show that pp125 is localized to focal adhesions; hence, we suggest the name focal adhesion kinase. |
Databáze: | OpenAIRE |
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