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
Rok vydání: 1992
Předmět:
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