Title: Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527.
Abstract: Research Article17 October 1994free access Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. K.B. Kaplan K.B. Kaplan Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author K.B. Bibbins K.B. Bibbins Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author J.R. Swedlow J.R. Swedlow Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author M. Arnaud M. Arnaud Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author D.O. Morgan D.O. Morgan Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author H.E. Varmus H.E. Varmus Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author K.B. Kaplan K.B. Kaplan Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author K.B. Bibbins K.B. Bibbins Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author J.R. Swedlow J.R. Swedlow Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author M. Arnaud M. Arnaud Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author D.O. Morgan D.O. Morgan Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author H.E. Varmus H.E. Varmus Department of Microbiology and Immunology, University of California, San Francisco 94143. Search for more papers by this author Author Information K.B. Kaplan1, K.B. Bibbins1, J.R. Swedlow1, M. Arnaud1, D.O. Morgan1 and H.E. Varmus1 1Department of Microbiology and Immunology, University of California, San Francisco 94143. The EMBO Journal (1994)13:4745-4756https://doi.org/10.1002/j.1460-2075.1994.tb06800.x PDFDownload PDF of article text and main figures. ToolsAdd to favoritesDownload CitationsTrack CitationsPermissions ShareFacebookTwitterLinked InMendeleyWechatReddit Figures & Info We have characterized the mechanism by which the subcellular distribution of c-Src is controlled by the phosphorylation of tyrosine 527. Mutation of this tyrosine dramatically redistributes c-Src from endosomal membranes to focal adhesions. Redistribution to focal adhesions occurs independently of kinase activity and cellular transformation. In cells lacking the regulatory kinase (CSK) that phosphorylates tyrosine 527, c-Src is also found predominantly in focal adhesions, confirming that phosphorylation of tyrosine 527 affects the location of c-Src inside the cell. The first 251 amino acids of c-Src are sufficient to allow association with focal adhesions, indicating that at least one signal for positioning c-Src in focal adhesions resides in the amino-terminal half. Point mutations and deletions in the first 251 amino acids of c-Src reveal that association with focal adhesions requires the myristylation site needed for membrane attachment, as well as the SH3 domain. Expression of the amino-terminal region alters both the structural and biochemical properties of focal adhesions. Focal adhesions containing this non-catalytic portion of c-Src are larger and exhibit increased levels of phosphotyrosine staining. Our results suggest that c-Src may regulate focal adhesions and cellular adhesion by a kinase-independent mechanism. Previous ArticleNext Article Volume 13Issue 201 October 1994In this issue RelatedDetailsLoading ...