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Proc Natl Acad Sci U S A. 2010 Aug 17;107(33):14591-6. doi: 10.1073/pnas.1007349107. Epub 2010 Aug 5.

In vitro and in vivo reconstitution of the cadherin-catenin-actin complex from Caenorhabditis elegans.

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1
Department of Biology, Stanford University, 318 Campus Drive, Stanford, CA 94305, USA.

Erratum in

  • Proc Natl Acad Sci U S A. 2011 Mar 8;108(10):4264.

Abstract

The ternary complex of cadherin, beta-catenin, and alpha-catenin regulates actin-dependent cell-cell adhesion. alpha-Catenin can bind beta-catenin and F-actin, but in mammals alpha-catenin either binds beta-catenin as a monomer or F-actin as a homodimer. It is not known if this conformational regulation of alpha-catenin is evolutionarily conserved. The Caenorhabditis elegans alpha-catenin homolog HMP-1 is essential for actin-dependent epidermal enclosure and embryo elongation. Here we show that HMP-1 is a monomer with a functional C-terminal F-actin binding domain. However, neither full-length HMP-1 nor a ternary complex of HMP-1-HMP-2(beta-catenin)-HMR-1(cadherin) bind F-actin in vitro, suggesting that HMP-1 is auto-inhibited. Truncation of either the F-actin or HMP-2 binding domain of HMP-1 disrupts C. elegans development, indicating that HMP-1 must be able to bind F-actin and HMP-2 to function in vivo. Our study defines evolutionarily conserved properties of alpha-catenin and suggests that multiple mechanisms regulate alpha-catenin binding to F-actin.

PMID:
20689042
PMCID:
PMC2930443
DOI:
10.1073/pnas.1007349107
[Indexed for MEDLINE]
Free PMC Article

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