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First published online 15 March 2005
doi: 10.1242/jcs.01734

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

Indra Chandrasekar¹, Theresia E. B. Stradal², Mark R. Holt³, Frank Entschladen⁴, Brigitte M. Jockusch¹ and Wolfgang H. Ziegler^1,*,

¹ Cell Biology, Zoological Institute, Technical University of Braunschweig, 38106 Braunschweig, Germany
² Cell Biology, German Research Centre for Biotechnology (GBF), 38124 Braunschweig, Germany
³ The Randall Division, King's College London, London SE1 1UL, UK
⁴ Institute of Immunology, Witten/Herdecke University, 58448, Witten, Germany

Author for correspondence (e-mail: wolfgang.ziegler{at}medizin.uni-leipzig.de)

Accepted 18 January 2005

The dynamics of cell adhesion sites control cell morphology and motility. Adhesion-site turnover is thought to depend on the local availability of the acidic phospholipid phosphatidylinositol-4,5-bisphosphate (PIP₂). PIP₂ can bind to many cell adhesion proteins such as vinculin and talin, but the consequences of this interaction are poorly understood. To study the significance of phospholipid binding to vinculin for adhesion-site turnover and cell motility, we constructed a mutant, vinculin-LD, deficient in acidic phospholipid binding yet with functional actin-binding sites. When expressed in cells, vinculin-LD was readily recruited to adhesion sites, as judged by fluorescence recovery after photobleaching (FRAP) analysis, but cell spreading and migration were strongly impaired, and PIP₂-dependent disassembly of adhesions was suppressed. Thus, PIP₂ binding is not essential for vinculin activation and recruitment, as previously suggested. Instead, we propose that PIP₂ levels can regulate the uncoupling of adhesion sites from the actin cytoskeleton, with vinculin functioning as a sensor.

Key words: Cell-matrix adhesion, Cell motility, Microfilaments, Phosphatidylinositol-4,5-bisphosphate, Vinculin

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