View : 861 Download: 0
Phospholipase C-γ1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation
- Title
- Phospholipase C-γ1 potentiates integrin-dependent cell spreading and migration through Pyk2/paxillin activation
- Authors
- Choi J.H.; Yang Y.-R.; Lee S.K.; Kim I.-S.; Ha S.H.; Kim E.-K.; Bae Y.S.; Ryu S.H.; Suh P.-G.
- Ewha Authors
- 배윤수
- SCOPUS Author ID
- 배윤수
- Issue Date
- 2007
- Journal Title
- Cellular Signalling
- ISSN
- 0898-6568
- Citation
- Cellular Signalling vol. 19, no. 8, pp. 1784 - 1796
- Indexed
- SCI; SCIE; SCOPUS
- Document Type
- Article
- 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.
- DOI
- 10.1016/j.cellsig.2007.04.002
- Appears in Collections:
- 자연과학대학 > 생명과학전공 > Journal papers
- Files in This Item:
There are no files associated with this item.
- Export
- RIS (EndNote)
- XLS (Excel)
- XML