| pubmed-article:10198051 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10198051 | lifeskim:mentions | umls-concept:C0379710 | lld:lifeskim |
| pubmed-article:10198051 | lifeskim:mentions | umls-concept:C1521991 | lld:lifeskim |
| pubmed-article:10198051 | lifeskim:mentions | umls-concept:C1880022 | lld:lifeskim |
| pubmed-article:10198051 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10198051 | pubmed:dateCreated | 1999-5-17 | lld:pubmed |
| pubmed-article:10198051 | pubmed:abstractText | Caveolin-1 was discovered as a major substrate for v-Src, but the effect of its tyrosine phosphorylation has not been known. We generated a specific antibody (PY14) to caveolin-1 phosphorylated at tyrosine 14 and studied the significance of the modification. By Western blotting of lysates of v-Src-expressing cells, PY14 recognized not only a 22-kDa band (the position of nonphosphorylated caveolin-1) but bands at 23-24 and 25 kDa. Bands of slower mobility were diminished by dephosphorylation and were also observed for mutant caveolin-1 lacking tyrosine 14. By immunofluorescence microscopy, PY14 did not label normal cells but detected large dots in v-Src-expressing cells. Immunoelectron microscopy revealed that the dots corresponded to aggregated caveolae and/or vesicles of various sizes; besides, the label was observed in intramembrane particle-free areas in the plasma membrane, which appeared to have been formed by fusion of flattened caveolae. A positive reaction with PY14 was found in normal cells after vanadate or pervanadate treatment; it occurred mainly at 22 kDa by Western blotting and was not seen as large dots by immunofluorescence microscopy. Detergent solubility, oligomerization, and association with caveolin-2 were observed similarly for caveolin-1 in normal and v-Src-expressing cells. The results indicate that phosphorylation of caveolin-1 in v-Src-expressing cells occurs at multiple residues and induces flattening, aggregation, and fusion of caveolae and/or caveolae-derived vesicles. | lld:pubmed |
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| pubmed-article:10198051 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10198051 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10198051 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10198051 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10198051 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:10198051 | pubmed:issn | 1059-1524 | lld:pubmed |
| pubmed-article:10198051 | pubmed:author | pubmed-author:FujimotoTT | lld:pubmed |
| pubmed-article:10198051 | pubmed:author | pubmed-author:NomuraRR | lld:pubmed |
| pubmed-article:10198051 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10198051 | pubmed:volume | 10 | lld:pubmed |
| pubmed-article:10198051 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10198051 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:10198051 | pubmed:pagination | 975-86 | lld:pubmed |
| pubmed-article:10198051 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
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| pubmed-article:10198051 | pubmed:meshHeading | pubmed-meshheading:10198051... | lld:pubmed |
| pubmed-article:10198051 | pubmed:year | 1999 | lld:pubmed |
| pubmed-article:10198051 | pubmed:articleTitle | Tyrosine-phosphorylated caveolin-1: immunolocalization and molecular characterization. | lld:pubmed |
| pubmed-article:10198051 | pubmed:affiliation | Department of Anatomy and Cell Biology, Gunma University School of Medicine, Maebashi 371-8511, Japan. | lld:pubmed |
| pubmed-article:10198051 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:10198051 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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