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First published online 18 August 2009
doi: 10.1242/jcs.054155

Journal of Cell Science 122, 3225-3232 (2009)
Published by The Company of Biologists 2009
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Short Report

Liprin-{alpha}1 promotes cell spreading on the extracellular matrix by affecting the distribution of activated integrins

Claudia Asperti, Veronica Astro, Antonio Totaro, Simona Paris and Ivan de Curtis*

Cell Adhesion Unit, Department of Neuroscience, San Raffaele University and San Raffaele Scientific Institute, 20132 Milano, Italy

* Author for correspondence (decurtis.ivan{at}hsr.it)

Accepted 2 July 2009

Summary

Integrin activation is needed to link the extracellular matrix with the actin cytoskeleton during cell motility. Protrusion requires coordination of actin dynamics with focal-adhesion turnover. We report that the adaptor protein liprin-{alpha}1 is stably associated with the cell membrane. Lipin-{alpha}1 shows a localization that is distinct from that of activated β1 integrins at the edge of spreading cells. Depletion of liprin-{alpha}1 inhibits the spreading of COS7 cells on fibronectin by affecting lamellipodia formation, whereas its overexpression enhances spreading, and lamellipodia and focal-adhesion formation at the cell edge. Cooperation between liprin-{alpha}1 and talin is needed, because either talin or liprin depletion prevents spreading in the presence of the other protein. The effects of liprin on spreading, but not its effects in the reorganization of the cell edge, are dependent on its interaction with leukocyte common antigen-related tyrosine phosphatase receptors. Therefore, liprin is an essential regulator of cell motility that contributes to the effectiveness of cell-edge protrusion.

Key words: Cell motility, Focal adhesions, Integrins, Talin


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