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DC Field | Value | Language |
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dc.citation.endPage | 8682 | - |
dc.citation.number | 29 | - |
dc.citation.startPage | 8674 | - |
dc.citation.title | BIOCHEMISTRY | - |
dc.citation.volume | 39 | - |
dc.contributor.author | Kim, Myung Jong | - |
dc.contributor.author | Chang, Jong-Soo | - |
dc.contributor.author | Park, Seung Kook | - |
dc.contributor.author | Hwang, Jong-Ik | - |
dc.contributor.author | Ryu, Sung Ho | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T12:07:20Z | - |
dc.date.available | 2023-12-22T12:07:20Z | - |
dc.date.created | 2015-08-17 | - |
dc.date.issued | 2000-07 | - |
dc.description.abstract | A recent report that microinjection of the SH3 domain of PLC-gamma 1 could induce DNA synthesis raised the functional importance of the SH3 domain of PLC-gamma 1 in mitogenic signaling. In this report, we provide evidence that SOS1, a p2Ras-specific guanine nucleotide exchange factor, directly binds to the SH3 domain of PLC-gamma 1, and that the SH3 domain of 1 is involved in SOS1-mediated p21Ras activation. SOS1 was coprecipitated with the GST-fused SH3 domain of PLC-gamma 1 in vitro. The interaction between SOS1 and the PLC-gamma 1 SH3 domain is mediated by direct physical interaction. The carboxyl-terminal proline-rich domain of SOS1 is involved in the interaction with the PLC-gamma 1 SH3 domain. Moreover, PLC-gamma 1 could be co-immunoprecipitated with SOS1 antibody in cell lysates. From transient expression studies, we could demonstrate that the SH3 domain of PLC-gamma 1 is necessary for the association with SOS1 in vivo. Intriguingly, overexpression of the SH3 domain of PLC-gamma 1, lipase-inactive PLC-gamma 1, or wild-type PLC-gamma 1 elevated p21Ras activity and ERK activity when compared with vector transfected cells. The PLC-gamma 1 mutant lacking the SH3 domain could not activate p21Ras. p21Ras activities in cell lines overexpressing either PLC-gamma 1 or the SH2-SH2-SH3 domain of PLC-gamma 1 were elevated about 2-fold compared to vector transfected cells. This study is the first to demonstrate that the PLC-gamma 1 SH3 domain enhances p21Ras activity, and that the SH3 domain of PLC-gamma 1 may be involved in the SOS1-mediated signaling pathway | - |
dc.identifier.bibliographicCitation | BIOCHEMISTRY, v.39, no.29, pp.8674 - 8682 | - |
dc.identifier.doi | 10.1021/bi992558t | - |
dc.identifier.issn | 0006-2960 | - |
dc.identifier.scopusid | 2-s2.0-0001550680 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/16526 | - |
dc.identifier.url | http://pubs.acs.org/doi/abs/10.1021/bi992558t | - |
dc.identifier.wosid | 000088376900037 | - |
dc.language | 영어 | - |
dc.publisher | AMER CHEMICAL SOC | - |
dc.title | Direct interaction of SOS1 ras exchange protein with the SH3 domain of phospholipase C-gamma 1 | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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