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MBC in Press, published online ahead of print January 12, 2005
Mol. Biol. Cell 10.1091/mbc.E04-08-0721

A more recent version of this article appeared on March 1, 2005
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Submitted on August 20, 2004
Revised on December 14, 2004
Accepted on December 16, 2004

Src-dependent Ezrin Phosphorylation in Adhesion-mediated Signaling

J. Srivastava,* B. E. Elliott,{dagger} D. Louvard,* and M. Arpin*{ddagger}

*Morphogenèse et Signalisation Cellulaires, CNRS-Institut Curie, 75248 Paris Cedex 05, France; {dagger}Queen’s University Cancer Research Institute, Division of Cancer Biology and Genetics, Kingston, Ontario K7L 3N6, Canada

Monitoring Editor: Richard Hynes

In addition to providing a regulated linkage between the membrane and the actin cytoskeleton, ezrin participates in signal transduction pathways. Here we describe that expression of the ezrin Y145F mutant delays epithelial cell spreading on fibronectin by inhibiting events leading to FAK activation. The defect in spreading was rescued by the overexpression of catalytically functional Src. We demonstrate that ezrin Y145 is phosphorylated in A431 cells stimulated with epidermal growth factor (EGF) and in v-Src transformed cells. Moreover in cells devoid of Src, SYF-/- fibroblasts, ezrin Y145 phosphorylation could only be detected upon the introduction of an active form of Src. The phosphorylation of ezrin at Y145 required prior binding of the Src SH2 domain to ezrin. Our results further show that Src activity influences its binding to ezrin and a positive feedback mechanism for Src-mediated Y145 phosphorylation is implied. Interestingly, cells expressing ezrin Y145F did not proliferate when cultured in a 3D collagen gel. Collectively, our results demonstrate a key signaling input of Src-dependent ezrin phosphorylation in adhesion-mediated events in epithelial cells.

{ddagger}Corresponding author. E-mail: marpin{at}curie.fr






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