Specific phosphorylation of p120-catenin regulatory domain differently modulates its binding to RhoA

Julio Castaño, Guiomar Solanas, David Casagolda, Imma Raurell, Patricia Villagrasa, Xosé R. Bustelo, Antonio Garcia De Herreros, Mireia Duñach

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91 Citations (Scopus)

Abstract

p120-catenin is an adherens junction-associated protein that controls E-cadherin function and stability. p120-catenin also binds intracellular proteins, such as the small GTPase RhoA. In this paper, we identify the p120-catenin N-terminal regulatory domain as the docking site for RhoA. Moreover, we demonstrate that the binding of RhoA to p120-catenin is tightly controlled by the Src family-dependent phosphorylation of p120-catenin on tyrosine residues. The phosphorylation induced by Src and Fyn tyrosine kinases on p120-catenin induces opposite elects on RhoA binding. Fyn, by phosphorylating a residue located in the regulatory domain of p120-catenin (Tyr112), inhibits the interaction of this protein with RhoA. By contrast, the phosphorylation of Tyr217 and Tyr228 by Src promotes a better affinity of p120-catenin towards RhoA. In agreement with these biochemical data, results obtained in cell lines support the important role of these phosphorylation sites in the regulation of RhoA activity by p120-catenin. Taken together, these observations uncover a new regulatory mechanism acting on p120-catenin that contributes to the fine-tuned regulation of the RhoA pathways during specific signaling events. Copyright © 2007, American Society for Microbiology. All Rights Reserved.
Original languageEnglish
Pages (from-to)1745-1757
JournalMolecular and Cellular Biology
Volume27
DOIs
Publication statusPublished - 1 Mar 2007

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