| pubmed-article:10675331 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:10675331 | lifeskim:mentions | umls-concept:C0080298 | lld:lifeskim |
| pubmed-article:10675331 | lifeskim:mentions | umls-concept:C0034802 | lld:lifeskim |
| pubmed-article:10675331 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
| pubmed-article:10675331 | lifeskim:mentions | umls-concept:C0038592 | lld:lifeskim |
| pubmed-article:10675331 | lifeskim:mentions | umls-concept:C2611812 | lld:lifeskim |
| pubmed-article:10675331 | lifeskim:mentions | umls-concept:C0851285 | lld:lifeskim |
| pubmed-article:10675331 | pubmed:issue | 4 | lld:pubmed |
| pubmed-article:10675331 | pubmed:dateCreated | 2000-3-20 | lld:pubmed |
| pubmed-article:10675331 | pubmed:abstractText | c-Src is a membrane-associated tyrosine kinase that can be activated by many types of extracellular signals, and can regulate the function of a variety of cellular protein substrates. We demonstrate that epidermal growth factor (EGF) and beta-adrenergic receptors activate c-Src by different mechanisms leading to the phosphorylation of distinct sets of c-Src substrates. In particular, we found that EGF receptors, but not beta(2)-adrenergic receptors, activated c-Src by a Ral-GTPase-dependent mechanism. Also, c-Src activated by EGF treatment or expression of constitutively activated Ral-GTPase led to tyrosine phosphorylation of Stat3 and cortactin, but not Shc or subsequent Erk activation. In contrast, c-Src activated by isoproterenol led to tyrosine phosphorylation of Shc and subsequent Erk activation, but not tyrosine phosphorylation of cortactin or Stat3. These results identify a role for Ral-GTPases in the activation of c-Src by EGF receptors and the coupling of EGF to transcription through Stat3 and the actin cytoskeleton through cortactin. They also show that c-Src kinase activity can be used differently by individual extracellular stimuli, possibly contributing to their ability to generate unique cellular responses. | lld:pubmed |
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| pubmed-article:10675331 | pubmed:language | eng | lld:pubmed |
| pubmed-article:10675331 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:10675331 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:10675331 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:10675331 | pubmed:month | Feb | lld:pubmed |
| pubmed-article:10675331 | pubmed:issn | 0261-4189 | lld:pubmed |
| pubmed-article:10675331 | pubmed:author | pubmed-author:NGJJ | lld:pubmed |
| pubmed-article:10675331 | pubmed:author | pubmed-author:FosterD ADA | lld:pubmed |
| pubmed-article:10675331 | pubmed:author | pubmed-author:KlinzS GSG | lld:pubmed |
| pubmed-article:10675331 | pubmed:author | pubmed-author:FeigL ALA | lld:pubmed |
| pubmed-article:10675331 | pubmed:author | pubmed-author:GoiTT | lld:pubmed |
| pubmed-article:10675331 | pubmed:author | pubmed-author:ShipitsinMM | lld:pubmed |
| pubmed-article:10675331 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:10675331 | pubmed:day | 15 | lld:pubmed |
| pubmed-article:10675331 | pubmed:volume | 19 | lld:pubmed |
| pubmed-article:10675331 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:10675331 | pubmed:authorsComplete | Y | lld:pubmed |
