E-cadherin/catenin complexes are formed cotranslationally in the endoplasmic reticulum/Golgi compartments

Cell Commun Adhes. 2008 Nov;15(4):365-78. doi: 10.1080/15419060802460748.

Abstract

Cadherins are synthesized with a proregion that lies between a short amino-terminal signal sequence and the first extracellular domain. Following synthesis, the proregion is cleaved, an event that is mandatory for the mature cadherin to function in adhesion. The authors have previously reported that catenins coimmunoprecipate with pro-N-cadherin, and that the N-cadherin/catenin complex forms in the Golgi/endoplasmic reticulum. It is clear that N- and E-cadherin confer significantly different characteristics on cells, and it is possible that N- and E-cadherin/catenin complex formation is equally different. To investigate this, the authors generated an antibody against the proregion of E-cadherin and have used it to examine the assembly of the E-cadherin/catenin complex.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • Biological Transport
  • Cadherins / biosynthesis
  • Cadherins / metabolism*
  • Catenins / biosynthesis
  • Catenins / metabolism*
  • Cell Adhesion Molecules / metabolism
  • Cell Membrane / metabolism
  • Cells, Cultured
  • Cytoskeleton / metabolism
  • Delta Catenin
  • Endoplasmic Reticulum / metabolism*
  • Golgi Apparatus / metabolism*
  • Humans
  • Immunoprecipitation
  • Phosphoproteins / metabolism
  • Protein Binding
  • Protein Biosynthesis

Substances

  • Cadherins
  • Catenins
  • Cell Adhesion Molecules
  • Phosphoproteins
  • Delta Catenin