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Cell. 2010 Apr 2;141(1):117-28. doi: 10.1016/j.cell.2010.01.017.

Dynamic and static interactions between p120 catenin and E-cadherin regulate the stability of cell-cell adhesion.

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  • 1Division of Signaling Biology, Ontario Cancer Institute, ON, Canada.

Abstract

The association of p120 catenin (p120) with the juxtamembrane domain (JMD) of the cadherin cytoplasmic tail is critical for the surface stability of cadherin-catenin cell-cell adhesion complexes. Here, we present the crystal structure of p120 isoform 4A in complex with the JMD core region (JMD(core)) of E-cadherin. The p120 armadillo repeat domain contains modular binding pockets that are complementary to electrostatic and hydrophobic properties of the JMD(core). Single-residue mutations within the JMD(core)-binding site of p120 abolished its interaction with E- and N-cadherins in vitro and in cultured cells. These mutations of p120 enabled us to clearly differentiate between N-cadherin-dependent and -independent steps of neuronal dendritic spine morphogenesis crucial for synapse development. NMR studies revealed that p120 regulates the stability of cadherin-mediated cell-cell adhesion by associating with the majority of the JMD, including residues implicated in clathrin-mediated endocytosis and Hakai-dependent ubiquitination of E-cadherin, through its discrete "dynamic" and "static" binding sites.

Copyright 2010 Elsevier Inc. All rights reserved.

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PMID:
20371349
[PubMed - indexed for MEDLINE]
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