Structure and Biochemistry of Cadherins and Catenins (original) (raw)

  1. Lawrence Shapiro1 and
  2. William I. Weis2
  3. 1Department of Biochemistry and Molecular Biophysics and Edward S. Harkness Eye Institute, Columbia University, New York, New York 10032
  4. 2Departments of Structural Biology, Molecular and Cellular Physiology, and Photon Science, Stanford University School of Medicine, Stanford, California 94305
  5. Correspondence: lss8{at}columbia.edu

Abstract

Classical cadherins mediate specific adhesion at intercellular adherens junctions. Interactions between cadherin ectodomains from apposed cells mediate cell–cell contact, whereas the intracellular region functionally links cadherins to the underlying cytoskeleton. Structural, biophysical, and biochemical studies have provided important insights into the mechanism and specificity of cell–cell adhesion by classical cadherins and their interplay with the cytoskeleton. Adhesive binding arises through exchange of β strands between the first extracellular cadherin domains (EC1) of partner cadherins from adjacent cells. This “strand-swap” binding mode is common to classical and desmosomal cadherins, but sequence alignments suggest that other cadherins will bind differently. The intracellular region of classical cadherins binds to p120 and β-catenin, and β-catenin binds to the F-actin binding protein α-catenin. Rather than stably bridging β-catenin to actin, it appears that α-catenin actively regulates the actin cytoskeleton at cadherin-based cell–cell contacts.

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