There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 3115 | - |
dc.citation.number | 9 | - |
dc.citation.startPage | 3103 | - |
dc.citation.title | MOLECULAR AND CELLULAR BIOLOGY | - |
dc.citation.volume | 23 | - |
dc.contributor.author | Ahn, Bong-Hyun | - |
dc.contributor.author | Kim, Shi Yeon | - |
dc.contributor.author | Kim, Eun Hee | - |
dc.contributor.author | Choi, Kyeong Sook | - |
dc.contributor.author | Kwon, Taeg Kyu | - |
dc.contributor.author | Lee, Young Han | - |
dc.contributor.author | Chang, Jong-Soo | - |
dc.contributor.author | Kim, Myung-Suk | - |
dc.contributor.author | Jo, Yang-Hyeok | - |
dc.contributor.author | Min, Do Sik | - |
dc.date.accessioned | 2023-12-22T11:12:06Z | - |
dc.date.available | 2023-12-22T11:12:06Z | - |
dc.date.created | 2016-08-02 | - |
dc.date.issued | 2003-05 | - |
dc.description.abstract | Phospholipase D (PLD) has been implicated in the signal transduction pathways initiated by several mitogenic protein tyrosine kinases. We demonstrate for the first time that most notably PLD2 and to a lesser extent the PLD1 isoform are tyrosine phosphorylated by c-Src tyrosine kinase via direct association. Moreover, epidermal growth factor induced tyrosine phosphorylation of PLD2 and its interaction with c-Src in A431 cells. Interaction between these proteins is via the pleckstrin homology domain of PLD2 and the catalytic domain of c-Src. Coexpression of PLD1 or PLD2 with c-Src synergistically enhances cellular proliferation compared with expression of either molecule. While PLD activity as a lipid-hydrolyzing enzyme is not affected by c-Src, wildtype PLDs but not catalytically inactive PLD mutants significantly increase c-Src kinase activity, up-regulating c-Src-mediated paxillin phosphorylation and extracellular signal-regulated kinase activity. These results demonstrate the critical role of PLD catalytic activity in the stimulation of Src signaling. In conclusion, we provide the first evidence that c-Src acts as a kinase of PLD and PLD acts as an activator of c-Src. This transmodulation between c-Src and PLD may contribute to the promotion of cellular proliferation via amplification of mitogenic signaling pathways | - |
dc.identifier.bibliographicCitation | MOLECULAR AND CELLULAR BIOLOGY, v.23, no.9, pp.3103 - 3115 | - |
dc.identifier.doi | 10.1128/MCB.23.9.3103-3115.2003 | - |
dc.identifier.issn | 0270-7306 | - |
dc.identifier.scopusid | 2-s2.0-0037405788 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/20190 | - |
dc.identifier.url | http://mcb.asm.org/content/23/9/3103 | - |
dc.identifier.wosid | 000182325500007 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.title | Transmodulation between phospholipase D and c-Src enhances cell proliferation | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.