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Dimer asymmetry defines α-catenin interactions

Academic Article
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Overview

authors

  • Rangarajan, E. S.
  • Izard, T.

publication date

  • February 2013

journal

  • Nature Structural & Molecular Biology  Journal

abstract

  • The F-actin-binding cytoskeletal protein α-catenin interacts with β-catenin-cadherin complexes and stabilizes cell-cell junctions. The β-catenin-α-catenin complex cannot bind F-actin, whereas interactions of α-catenin with the cytoskeletal protein vinculin appear to be necessary to stabilize adherens junctions. Here we report the crystal structure of nearly full-length human α-catenin at 3.7-Å resolution. α-catenin forms an asymmetric dimer where the four-helix bundle domains of each subunit engage in distinct intermolecular interactions. This results in a left handshake-like dimer, wherein the two subunits have remarkably different conformations. The crystal structure explains why dimeric α-catenin has a higher affinity for F-actin than does monomeric α-catenin, why the β-catenin-α-catenin complex does not bind F-actin, how activated vinculin links the cadherin-catenin complex to the cytoskeleton and why α-catenin but not inactive vinculin can bind F-actin.

subject areas

  • Actins
  • Adherens Junctions
  • Chromatography, Gel
  • Crystallography, X-Ray
  • Dimerization
  • Electrophoretic Mobility Shift Assay
  • Humans
  • Immunoblotting
  • Models, Molecular
  • Protein Conformation
  • Vinculin
  • X-Ray Diffraction
  • alpha Catenin
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Identity

PubMed Central ID

  • PMC3805043

International Standard Serial Number (ISSN)

  • 1545-9993

Digital Object Identifier (DOI)

  • 10.1038/nsmb.2479

PubMed ID

  • 23292143
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Additional Document Info

start page

  • 188

end page

  • 193

volume

  • 20

issue

  • 2

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