| pubmed-article:11805080 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0035820 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0138965 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0379710 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0031715 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0041485 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0271510 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C1704675 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C0430054 | lld:lifeskim |
| pubmed-article:11805080 | lifeskim:mentions | umls-concept:C1705053 | lld:lifeskim |
| pubmed-article:11805080 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:11805080 | pubmed:dateCreated | 2002-3-11 | lld:pubmed |
| pubmed-article:11805080 | pubmed:abstractText | Caveolin-1 is a substrate for nonreceptor tyrosine kinases including Src, Fyn, and Abl. To investigate the function of caveolin-1 phosphorylation, we modified the Gal4-based yeast two-hybrid system to screen for phosphorylation-dependent protein interactions. A cDNA library was screened using the N terminus of caveolin-1 as bait in a yeast strain expressing the catalytic domain of Abl. We identified two proteins in this screen that interact with caveolin-1 in a phosphorylation-dependent manner: tumor necrosis factor-alpha receptor-associated factor 2 (TRAF2) and C-terminal Src kinase (Csk). TRAF2 bound to nonphosphorylated caveolin-1, but this association was increased 3-fold by phosphorylation. In contrast, association of Csk with caveolin-1 was completely dependent on phosphorylation of caveolin-1, both for fusion proteins in yeast (>35-fold difference in affinity) and for endogenous proteins in tissue culture cells. Our data suggest that phosphorylation of caveolin-1 leads to Csk translocation into caveolae. This may induce a feedback loop that leads to inactivation of the Src family kinases that are highly enriched in caveolae. | lld:pubmed |
| pubmed-article:11805080 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:11805080 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:11805080 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:11805080 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:11805080 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:11805080 | pubmed:month | Mar | lld:pubmed |
| pubmed-article:11805080 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:11805080 | pubmed:author | pubmed-author:CourchesneWil... | lld:pubmed |
| pubmed-article:11805080 | pubmed:author | pubmed-author:MastickCynthi... | lld:pubmed |
| pubmed-article:11805080 | pubmed:author | pubmed-author:CaoHaimingH | lld:pubmed |
| pubmed-article:11805080 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:11805080 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:11805080 | pubmed:volume | 277 | lld:pubmed |
| pubmed-article:11805080 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:11805080 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:11805080 | pubmed:pagination | 8771-4 | lld:pubmed |
| pubmed-article:11805080 | pubmed:dateRevised | 2011-11-2 | lld:pubmed |
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| pubmed-article:11805080 | pubmed:meshHeading | pubmed-meshheading:11805080... | lld:pubmed |
| pubmed-article:11805080 | pubmed:year | 2002 | lld:pubmed |
| pubmed-article:11805080 | pubmed:articleTitle | A phosphotyrosine-dependent protein interaction screen reveals a role for phosphorylation of caveolin-1 on tyrosine 14: recruitment of C-terminal Src kinase. | lld:pubmed |
| pubmed-article:11805080 | pubmed:affiliation | Department of Biochemistry, University of Nevada, Reno, Nevada 89557, USA. | lld:pubmed |
| pubmed-article:11805080 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:11805080 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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