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First published online March 23, 2005

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Make and break: the vinculin-lipid connection

The turnover of small transient cell-matrix adhesion sites, which is required for cell spreading and migration, is thought to depend on local phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P₂] concentrations. Previous studies have suggested that the binding of PtdIns(4,5)P₂ to vinculin, a structural component of adhesion sites, promotes vinculin's activation and targeting to adhesion sites, where it binds talin and actin. On p. 1461, Wolfgang Ziegler and colleagues challenge this idea, showing that it is adhesion-site turnover rather than vinculin targeting that depends on the PtdIns(4,5)P₂-vinculin interaction. The authors have constructed vinculin-LD, a vinculin mutant lacking PtdIns(4,5)P₂-binding sites, and expressed it in a mouse melanoma cell line. Vinculin-LD is readily recruited to adhesion sites but adhesion-site turnover is reduced, resulting in impaired cell spreading and migration. Furthermore, vinculin-LD expression suppresses the disassembly of adhesion sites and cell detachment usually seen when PtdIns(4,5)P₂ levels are increased by overexpression of PIP 5-kinase. Vinculin, the authors conclude, is a sensor that converts local modulation of PtdIns(4,5)P₂ levels into adhesion-site dynamics.

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Vinculin acts as a sensor in lipid regulation of adhesion-site turnover

Indra Chandrasekar, Theresia E. B. Stradal, Mark R. Holt, Frank Entschladen, Brigitte M. Jockusch, and Wolfgang H. Ziegler
JCS 2005 118: 1461-1472. [Abstract] [Full Text]  

This Article Full Text (PDF) Alert me when this article is cited Alert me if a correction is posted Services Email this article to a friend Related articles in JCS Similar articles in this journal Alert me to new issues of the journal Download to citation manager Citing Articles Citing Articles via Google Scholar Google Scholar Search for Related Content