| pubmed-article:7525268 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0080298 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0887870 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C2825407 | lld:lifeskim |
| pubmed-article:7525268 | lifeskim:mentions | umls-concept:C0871161 | lld:lifeskim |
| pubmed-article:7525268 | pubmed:issue | 20 | lld:pubmed |
| pubmed-article:7525268 | pubmed:dateCreated | 1994-12-1 | lld:pubmed |
| pubmed-article:7525268 | pubmed:abstractText | 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. | lld:pubmed |
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| pubmed-article:7525268 | pubmed:language | eng | lld:pubmed |
| pubmed-article:7525268 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:7525268 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:7525268 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:7525268 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:7525268 | pubmed:month | Oct | lld:pubmed |
| pubmed-article:7525268 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:7525268 | pubmed:author | pubmed-author:MorganD ODO | lld:pubmed |
| pubmed-article:7525268 | pubmed:author | pubmed-author:ArnaudMM | lld:pubmed |
| pubmed-article:7525268 | pubmed:author | pubmed-author:VarmusH EHE | lld:pubmed |
| pubmed-article:7525268 | pubmed:author | pubmed-author:KaplanK BKB | lld:pubmed |
| pubmed-article:7525268 | pubmed:author | pubmed-author:SwedlowJ RJR | lld:pubmed |
| pubmed-article:7525268 | pubmed:author | pubmed-author:BibbinsK BKB | lld:pubmed |
| pubmed-article:7525268 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:7525268 | pubmed:day | 17 | lld:pubmed |
| pubmed-article:7525268 | pubmed:volume | 13 | lld:pubmed |
| pubmed-article:7525268 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:7525268 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:7525268 | pubmed:pagination | 4745-56 | lld:pubmed |
| pubmed-article:7525268 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:7525268 | pubmed:meshHeading | pubmed-meshheading:7525268-... | lld:pubmed |
| pubmed-article:7525268 | pubmed:year | 1994 | lld:pubmed |
| pubmed-article:7525268 | pubmed:articleTitle | Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. | lld:pubmed |
| pubmed-article:7525268 | pubmed:affiliation | Department of Microbiology and Immunology, University of California, San Francisco 94143. | lld:pubmed |
