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DC Field | Value | Language |
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dc.citation.endPage | 1796 | - |
dc.citation.number | 8 | - |
dc.citation.startPage | 1784 | - |
dc.citation.title | CELLULAR SIGNALLING | - |
dc.citation.volume | 19 | - |
dc.contributor.author | Choi, Jang Hyun | - |
dc.contributor.author | Yang, Yong-Ryoul | - |
dc.contributor.author | Lee, Seul Ki | - |
dc.contributor.author | Kim, Il-Shin | - |
dc.contributor.author | Ha, Sang Hoon | - |
dc.contributor.author | Kim, Eung-Kyun | - |
dc.contributor.author | Bae, Yun Soo | - |
dc.contributor.author | Ryu, Sung Ho | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.date.accessioned | 2023-12-22T09:11:36Z | - |
dc.date.available | 2023-12-22T09:11:36Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2007-08 | - |
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. | - |
dc.identifier.bibliographicCitation | CELLULAR SIGNALLING, v.19, no.8, pp.1784 - 1796 | - |
dc.identifier.doi | 10.1016/j.cellsig.2007.04.002 | - |
dc.identifier.issn | 0898-6568 | - |
dc.identifier.scopusid | 2-s2.0-34250639027 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5661 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=34250639027 | - |
dc.identifier.wosid | 000248175200017 | - |
dc.language | 영어 | - |
dc.publisher | ELSEVIER SCIENCE INC | - |
dc.title | Phospholipase C-gamma 1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | phospholipase C-gamma l | - |
dc.subject.keywordAuthor | pyk2 | - |
dc.subject.keywordAuthor | paxillin | - |
dc.subject.keywordAuthor | rac1 | - |
dc.subject.keywordAuthor | integrin | - |
dc.subject.keywordAuthor | adhesion | - |
dc.subject.keywordAuthor | migration | - |
dc.subject.keywordPlus | FOCAL ADHESION KINASE | - |
dc.subject.keywordPlus | RICH TYROSINE KINASE-2 | - |
dc.subject.keywordPlus | GROWTH-FACTOR RECEPTOR | - |
dc.subject.keywordPlus | ACTIN STRESS FIBERS | - |
dc.subject.keywordPlus | C-GAMMA-L | - |
dc.subject.keywordPlus | DIFFERENTIAL REGULATION | - |
dc.subject.keywordPlus | INVASION | - |
dc.subject.keywordPlus | PHOSPHORYLATION | - |
dc.subject.keywordPlus | MOTILITY | - |
dc.subject.keywordPlus | RAC | - |
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