| pubmed-article:12803489 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:12803489 | lifeskim:mentions | umls-concept:C0221920 | lld:lifeskim |
| pubmed-article:12803489 | lifeskim:mentions | umls-concept:C0031671 | lld:lifeskim |
| pubmed-article:12803489 | lifeskim:mentions | umls-concept:C0018270 | lld:lifeskim |
| pubmed-article:12803489 | lifeskim:mentions | umls-concept:C1879547 | lld:lifeskim |
| pubmed-article:12803489 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:12803489 | pubmed:dateCreated | 2003-6-13 | lld:pubmed |
| pubmed-article:12803489 | pubmed:abstractText | Phospholipase C-gamma1 (PLC-gamma1) plays pivotal roles in cellular growth and proliferation through its two Src homology (SH) 2 domains and its single SH3 domain, which interact with signaling molecules in response to various growth factors and hormones. However, the role of the SH domains in the growth factor-induced regulation of PLC-gamma1 is unclear. By peptide-mass fingerprinting analysis we have identified Cbl as a binding protein for the SH3 domain of PLC-gamma1 from rat pheochromatocyte PC12 cells. Association of Cbl with PLC-gamma1 was induced by epidermal growth factor (EGF) but not by nerve growth factor (NGF). Upon EGF stimulation, both Cbl and PLC-gamma1 were recruited to the activated EGF receptor through their SH2 domains. Mutation of the SH2 domains of either Cbl or PLC-gamma1 abrogated the EGF-induced interaction of PLC-gamma1 with Cbl, indicating that SH2-mediated translocation is essential for the association of PLC-gamma1 and Cbl. Overexpression of Cbl attenuated EGF-induced tyrosine phosphorylation and the subsequent activation of PLC-gamma1 by interfering competitively with the interaction between PLC-gamma1 and EGFR. Taken together, these results provide the first indications that Cbl may be a negative regulator of intracellular signaling following EGF-induced PLC-gamma1 activation. | lld:pubmed |
| pubmed-article:12803489 | pubmed:language | eng | lld:pubmed |
| pubmed-article:12803489 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12803489 | pubmed:citationSubset | IM | lld:pubmed |
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| pubmed-article:12803489 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:12803489 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:12803489 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:12803489 | pubmed:issn | 1016-8478 | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:RyuSung HoSH | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:SuhPann-Ghill... | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:CoccoLucioL | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:BaeSun SikSS | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:ParkJong... | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:ChoiJang... | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:SongHebokH | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:KimJae-HoJH | lld:pubmed |
| pubmed-article:12803489 | pubmed:author | pubmed-author:HaSang HoonSH | lld:pubmed |
| pubmed-article:12803489 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:12803489 | pubmed:day | 30 | lld:pubmed |
| pubmed-article:12803489 | pubmed:volume | 15 | lld:pubmed |
| pubmed-article:12803489 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:12803489 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:12803489 | pubmed:pagination | 245-55 | lld:pubmed |
| pubmed-article:12803489 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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| pubmed-article:12803489 | pubmed:meshHeading | pubmed-meshheading:12803489... | lld:pubmed |
| pubmed-article:12803489 | pubmed:year | 2003 | lld:pubmed |
| pubmed-article:12803489 | pubmed:articleTitle | Cbl competitively inhibits epidermal growth factor-induced activation of phospholipase C-gamma1. | lld:pubmed |
| pubmed-article:12803489 | pubmed:affiliation | Division of Molecular and Life Science, Pohang University of Science and Technology, Pohang 790-784, Korea. | lld:pubmed |
| pubmed-article:12803489 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:12803489 | pubmed:publicationType | In Vitro | lld:pubmed |
| pubmed-article:12803489 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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