Journal
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
Volume 107, Issue 33, Pages 14591-14596Publisher
NATL ACAD SCIENCES
DOI: 10.1073/pnas.1007349107
Keywords
cell-cell adhesion; HMP-1; HMP-2; HMR-1
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Funding
- Ruth L. Kirschstein National Research Service Award [5T32 CA09302]
- American Heart Association [0815662G]
- National Institutes of Health (NIH) [5T32 GM07133, GM058038, GM035527, GM56169]
- US Department of Energy
- National Institute of General Medical Sciences (NIGMS)
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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 ofHMP-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.
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