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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
20
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pubmed:dateCreated |
1994-12-1
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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.
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1370711,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1374414,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1378446,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1383278,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1384654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1423600,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1645450,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1689455,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1696179,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1702788,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1703304,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1705002,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1709169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1720334,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1720546,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-1997203,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2108315,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2118142,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2411538,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2415973,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2419901,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2450676,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2460746,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2461946,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2470513,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2474758,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2494418,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2981363,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-2991884,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-3031677,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-3103925,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-3103926,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-6192323,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-6251461,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-6251464,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-6256755,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-6291037,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7504171,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7505391,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7683128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7685657,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7687537,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7689147,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-7689149,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-8248193,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-8325872,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-8402898,
http://linkedlifedata.com/resource/pubmed/commentcorrection/7525268-8438166
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Oct
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pubmed:issn |
0261-4189
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
13
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
4745-56
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:7525268-Amino Acid Sequence,
pubmed-meshheading:7525268-Animals,
pubmed-meshheading:7525268-Biological Transport,
pubmed-meshheading:7525268-Cell Adhesion Molecules,
pubmed-meshheading:7525268-Cell Line,
pubmed-meshheading:7525268-Mice,
pubmed-meshheading:7525268-Molecular Sequence Data,
pubmed-meshheading:7525268-Phosphorylation,
pubmed-meshheading:7525268-Protein Binding,
pubmed-meshheading:7525268-Protein Sorting Signals,
pubmed-meshheading:7525268-Proto-Oncogene Proteins pp60(c-src),
pubmed-meshheading:7525268-Structure-Activity Relationship,
pubmed-meshheading:7525268-Subcellular Fractions,
pubmed-meshheading:7525268-Tyrosine
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pubmed:year |
1994
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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.
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pubmed:affiliation |
Department of Microbiology and Immunology, University of California, San Francisco 94143.
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