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| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C0242275 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C0037083 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C0085536 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C1335280 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C1706044 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C1179132 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C0293442 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C1710082 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C1710236 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:15133037 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:15133037 | pubmed:issue | 28 | lld:pubmed |
| pubmed-article:15133037 | pubmed:dateCreated | 2004-7-5 | lld:pubmed |
| pubmed-article:15133037 | pubmed:abstractText | The catalytic activity of the Src homology 2 (SH2) domain-containing tyrosine phosphatase, SHP-2, is required for virtually all of its signaling effects. Elucidating the molecular mechanisms of SHP-2 signaling, therefore, rests upon the identification of its target substrates. In this report, we have used SHP-2 substrate-trapping mutants to identify the major vault protein (MVP) as a putative SHP-2 substrate. MVP is the predominant component of vaults that are cytoplasmic ribonucleoprotein complexes of unknown function. We show that MVP is dephosphorylated by SHP-2 in vitro and it forms an enzyme-substrate complex with SHP-2 in vivo. In response to epidermal growth factor (EGF), SHP-2 associates via its SH2 domains with tyrosyl-phosphorylated MVP. MVP also interacts with the activated form of the extracellular-regulated kinases (Erks) in response to EGF and a constitutive complex between tyrosyl-phosphorylated MVP, SHP-2, and the Erks was detected in MCF-7 breast cancer cells. Using MVP-deficient fibroblasts, we demonstrate that MVP cooperates with Ras for optimal EGF-induced Elk-1 activation and is required for cell survival. We propose that MVP functions as a novel scaffold protein for both SHP-2 and Erk. The regulation of MVP tyrosyl phosphorylation by SHP-2 may play an important role in cell survival signaling. | lld:pubmed |
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| pubmed-article:15133037 | pubmed:language | eng | lld:pubmed |
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| pubmed-article:15133037 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:15133037 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:15133037 | pubmed:month | Jul | lld:pubmed |
| pubmed-article:15133037 | pubmed:issn | 0021-9258 | lld:pubmed |
| pubmed-article:15133037 | pubmed:author | pubmed-author:WiemerErik... | lld:pubmed |
| pubmed-article:15133037 | pubmed:author | pubmed-author:MossinkMariek... | lld:pubmed |
| pubmed-article:15133037 | pubmed:author | pubmed-author:BennettAnton... | lld:pubmed |
| pubmed-article:15133037 | pubmed:author | pubmed-author:KolliSivanaga... | lld:pubmed |
| pubmed-article:15133037 | pubmed:author | pubmed-author:ZitoChristina... | lld:pubmed |
| pubmed-article:15133037 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:15133037 | pubmed:day | 9 | lld:pubmed |
| pubmed-article:15133037 | pubmed:volume | 279 | lld:pubmed |
| pubmed-article:15133037 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:15133037 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:15133037 | pubmed:pagination | 29374-85 | lld:pubmed |
| pubmed-article:15133037 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:15133037 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:15133037 | pubmed:articleTitle | The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling. | lld:pubmed |
| pubmed-article:15133037 | pubmed:affiliation | Department of Pharmacology, Yale University School of Medicine, New Haven, Connecticut 06520-8066, USA. | lld:pubmed |
| pubmed-article:15133037 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:15133037 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
| pubmed-article:15133037 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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