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Published 24 October 2005. doi:10.1083/jcb.200503017
The Rockefeller University Press, 0021-9525 $8.00
JCB, Volume 171, Number 2, 383-392
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Article

The mechanisms and dynamics of {alpha}vß3 integrin clustering in living cells



Caroline Cluzel1, Frédéric Saltel1, Jost Lussi2, Frédérique Paulhe1, Beat A. Imhof1, and Bernhard Wehrle-Haller1

1 Department of Pathology and Immunlogy, Centre Medical Universitaire, 1211 Geneva 4, Switzerland
2 Bio Micro Metrics Group, Swiss Federal Institute of Technology, CH-8092 Zürich, Switzerland

Correspondence to Bernhard Wehrle-Haller: Bernhard.Wehrle-Haller{at}medecine.unige.ch

During cell migration, the physical link between the extracellular substrate and the actin cytoskeleton mediated by receptors of the integrin family is constantly modified. We analyzed the mechanisms that regulate the clustering and incorporation of activated {alpha}vß3 integrins into focal adhesions. Manganese (Mn2+) or mutational activation of integrins induced the formation of de novo F-actin–independent integrin clusters. These clusters recruited talin, but not other focal adhesion adapters, and overexpression of the integrin-binding head domain of talin increased clustering. Integrin clustering required immobilized ligand and was prevented by the sequestration of phosphoinositole-4,5-bisphosphate (PI(4,5)P2). Fluorescence recovery after photobleaching analysis of Mn2+-induced integrin clusters revealed increased integrin turnover compared with mature focal contacts, whereas stabilization of the open conformation of the integrin ectodomain by mutagenesis reduced integrin turnover in focal contacts. Thus, integrin clustering requires the formation of the ternary complex consisting of activated integrins, immobilized ligands, talin, and PI(4,5)P2. The dynamic remodeling of this ternary complex controls cell motility.

C. Cluzel and F. Saltel contributed equally to this paper.

C. Cluzel's present address is Institut de Biologie et Chimie des Proteines, Lyon Cedex 07, France.

F. Saltel, F. Paulhe, and B. Wehrle-Haller's present address is Dept. of Cellular Physiology and Metabolism, Centre Medical Universitaire, 1211 Geneva 4, Switzerland.

Abbreviations used in this paper: cRGD, cyclic RGD; cD, cytochalasin D; IRM, interference reflection microscopy; PI(4,5)P2, phosphoinositol-4,5-bisphosphate; TIRF, total internal reflection fluorescence; WT, wild type.


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