期刊
NATURE CELL BIOLOGY
卷 8, 期 8, 页码 803-U35出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/ncb1437
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资金
- NHLBI NIH HHS [HL19429] Funding Source: Medline
FilGAP is a newly recognized filamin A ( FLNa)-binding RhoGTPase-activating protein. The GTPase-activating protein ( GAP) activity of FilGAP is specific for Rac and FLNa binding targets FilGAP to sites of membrane protrusion, where it antagonizes Rac in vivo. Dominant-negative FilGAP constructs lacking GAP activity or knockdown of endogenous FilGAP by small interference RNA ( siRNA) induce spontaneous lamellae formation and stimulate cell spreading on fibronectin. Knockdown of endogenous FilGAP abrogates ROCK-dependent suppression of lamellae. Conversely, forced expression of FilGAP induces numerous blebs around the cell periphery and a ROCK-specific inhibitor suppresses bleb formation. ROCK phosphorylates FilGAP, and this phosphorylation stimulates its RacGAP activity and is a requirement for FilGAP-mediated bleb formation. FilGAP is, therefore, a mediator of the well-established antagonism of Rac by RhoA that suppresses leading edge protrusion and promotes cell retraction to achieve cellular polarity.
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