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DC Field | Value | Language |
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dc.citation.endPage | 1299 | - |
dc.citation.number | 10 | - |
dc.citation.startPage | 1289 | - |
dc.citation.title | CELLULAR SIGNALLING | - |
dc.citation.volume | 17 | - |
dc.contributor.author | Choi, Jang Hyun | - |
dc.contributor.author | Hong, WP | - |
dc.contributor.author | Yun, S | - |
dc.contributor.author | Kim, HS | - |
dc.contributor.author | Lee, JR | - |
dc.contributor.author | Park, JB | - |
dc.contributor.author | Bae, YS | - |
dc.contributor.author | Ryu, SH | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T10:12:26Z | - |
dc.date.available | 2023-12-22T10:12:26Z | - |
dc.date.created | 2014-10-14 | - |
dc.date.issued | 2005-10 | - |
dc.description.abstract | Phospholipase C-γ1 (PLC-γ1) plays pivotal roles in cellular growth and proliferation. Upon the stimulation of growth factors and hormones, PLC-γ1 is rapidly phosphorylated at three known sites; Tyr771, Tyr783 and Tyr1254 and its enzymatic activity is up-regulated. In this study, we demonstrate for the first time that Grb2, an adaptor protein, specifically interacts with tyrosine-phosphorylated PLC-γ1 at Tyr783. The association of Grb2 with PLC-γ1 was induced by the treatment with epidermal growth factor (EGF). Replacement of Tyr783 with Phe completely blocked EGF-induced interaction of PLC-γ1 with Grb2, indicating that tyrosine phosphorylation of PLC-γ1 at Tyr783 is essential for the interaction with Grb2. Interestingly, the depletion of Grb2 from HEK-293 cells by RNA interference significantly enhanced increased EGF-induced PLC-γ1 enzymatic activity and mobilization of the intracellular Ca2+, while it did not affect EGF-induced tyrosine phosphorylation of PLC-γ1. Furthermore, overexpression of Grb2 inhibited PLC-γ1 enzymatic activity. Taken together, these results suggest Grb2, in addition to its key function in signaling through Ras, may have a negatively regulatory role on EGF-induced PLC-γ1 activation. | - |
dc.identifier.bibliographicCitation | CELLULAR SIGNALLING, v.17, no.10, pp.1289 - 1299 | - |
dc.identifier.doi | 10.1016/j.cellsig.2005.01.005 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.scopusid | 2-s2.0-22144486622 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/7271 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=22144486622 | - |
dc.identifier.wosid | 000231182900012 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
dc.title | Grb2 negatively regulates epidermal growth factor-induced phospholipase C-gamma 1 activity through the direct interaction with tyrosine-phosphorylated phospholipase C-gamma 1 | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | phospholipase c-gamma 1 | - |
dc.subject.keywordAuthor | Grb2 | - |
dc.subject.keywordAuthor | tyrosine phosphorylation | - |
dc.subject.keywordAuthor | epidermal growth factor | - |
dc.subject.keywordAuthor | interaction | - |
dc.subject.keywordAuthor | suppression | - |
dc.subject.keywordPlus | C-GAMMA | - |
dc.subject.keywordPlus | EGF-RECEPTOR | - |
dc.subject.keywordPlus | NUCLEOTIDE EXCHANGE | - |
dc.subject.keywordPlus | INSULIN-RECEPTOR | - |
dc.subject.keywordPlus | ADAPTER PROTEIN | - |
dc.subject.keywordPlus | RAS | - |
dc.subject.keywordPlus | ACTIVATION | - |
dc.subject.keywordPlus | KINASE | - |
dc.subject.keywordPlus | ASSOCIATION | - |
dc.subject.keywordPlus | SEQUENCE | - |
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