pp125FAK a structurally distinctive protein-tyrosine kinase associated with focal adhesions.

Michael D. Schaller(University of Virginia), Cheryl A. Borgman(St. Jude Children's Research Hospital), Bradley S. Cobb(St. Jude Children's Research Hospital), R R Vines(St. Jude Children's Research Hospital), Albert B. Reynolds(University of Virginia), J. Thomas Parsons(St. Jude Children's Research Hospital)
Proceedings of the National Academy of Sciences
June 1, 1992
Cited by 1,443Open Access

Abstract

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.


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