Full metadata record
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 배윤수 | * |
dc.date.accessioned | 2017-02-15T08:02:32Z | - |
dc.date.available | 2017-02-15T08:02:32Z | - |
dc.date.issued | 2007 | * |
dc.identifier.issn | 0898-6568 | * |
dc.identifier.other | OAK-4147 | * |
dc.identifier.uri | https://dspace.ewha.ac.kr/handle/2015.oak/234405 | - |
dc.description.abstract | Phospholipase C-γ1 (PLC-γ1), which generates two second messengers, namely, inositol-1, 4, 5-trisphosphate and diacylglycerol, is implicated in growth factor-mediated chemotaxis. However, the exact role of PLC-γ1 in integrin-mediated cell adhesion and migration remains poorly understood. In this study, we demonstrate that PLC-γ1 is required for actin cytoskeletal organization and cell motility through the regulation of Pyk2 and paxillin activation. After fibronectin stimulation, PLC-γ1 directly interacted with the cytoplasmic tail of integrin β1. In PLC-γ1-silenced cells, integrin-induced Pyk2 and paxillin phosphorylation were significantly reduced and PLC-γ1 potentiated the integrin-induced Pyk2/paxillin activation in its enzymatic activity-dependent manner. In addition, specific knock-down of PLC-γ1 resulted in a failure to form focal adhesions dependent on fibronectin stimulation, which appeared to be caused by the suppression of Pyk2 and paxillin phosphorylation. Interestingly, PLC-γ1 potentiated the activations of Rac, thus integrin-induced lamellipodia formation was up-regulated. Consequently, the strength of cell-substratum interaction and cell motility were profoundly up-regulated by PLC-γ1. Taken together, these results suggest that PLC-γ1 is a key player in integrin-mediated cell spreading and motility achieved by the activation of Pyk2/paxillin/Rac signaling. © 2007 Elsevier Inc. All rights reserved. | * |
dc.language | English | * |
dc.title | Phospholipase C-γ1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation | * |
dc.type | Article | * |
dc.relation.issue | 8 | * |
dc.relation.volume | 19 | * |
dc.relation.index | SCI | * |
dc.relation.index | SCIE | * |
dc.relation.index | SCOPUS | * |
dc.relation.startpage | 1784 | * |
dc.relation.lastpage | 1796 | * |
dc.relation.journaltitle | Cellular Signalling | * |
dc.identifier.doi | 10.1016/j.cellsig.2007.04.002 | * |
dc.identifier.wosid | WOS:000248175200017 | * |
dc.identifier.scopusid | 2-s2.0-34250639027 | * |
dc.author.google | Choi J.H. | * |
dc.author.google | Yang Y.-R. | * |
dc.author.google | Lee S.K. | * |
dc.author.google | Kim I.-S. | * |
dc.author.google | Ha S.H. | * |
dc.author.google | Kim E.-K. | * |
dc.author.google | Bae Y.S. | * |
dc.author.google | Ryu S.H. | * |
dc.author.google | Suh P.-G. | * |
dc.contributor.scopusid | 배윤수(15031067200) | * |
dc.date.modifydate | 20240415133331 | * |