Nectin/PRR: an immunoglobulin-like cell adhesion molecule recruited to cadherin-based adherens junctions through interaction with Afadin, a PDZ domain-containing protein

J Cell Biol. 1999 May 3;145(3):539-49. doi: 10.1083/jcb.145.3.539.

Abstract

We have isolated a novel actin filament-binding protein, named afadin, localized at cadherin-based cell-cell adherens junctions (AJs) in various tissues and cell lines. Afadin has one PDZ domain, three proline-rich regions, and one actin filament-binding domain. We found here that afadin directly interacted with a family of the immunoglobulin superfamily, which was isolated originally as the poliovirus receptor-related protein (PRR) family consisting of PRR1 and -2, and has been identified recently to be the alphaherpes virus receptor. PRR has a COOH-terminal consensus motif to which the PDZ domain of afadin binds. PRR and afadin were colocalized at cadherin-based cell-cell AJs in various tissues and cell lines. In E-cadherin-expressing EL cells, PRR was recruited to cadherin-based cell-cell AJs through interaction with afadin. PRR showed Ca2+-independent cell-cell adhesion activity. These results indicate that PRR is a cell-cell adhesion molecule of the immunoglobulin superfamily which is recruited to cadherin-based cell-cell AJs through interaction with afadin. We rename PRR as nectin (taken from the Latin word "necto" meaning "to connect").

MeSH terms

  • Alternative Splicing / genetics
  • Amino Acid Sequence
  • Animals
  • COS Cells / chemistry
  • COS Cells / metabolism
  • Cadherins / metabolism*
  • Calcium / metabolism
  • Cell Adhesion Molecules / chemistry
  • Cell Adhesion Molecules / genetics*
  • Cell Adhesion Molecules / metabolism
  • Cell Aggregation / physiology
  • Epithelial Cells / chemistry
  • Epithelial Cells / cytology
  • Epithelial Cells / metabolism
  • Intercellular Junctions / chemistry
  • Intercellular Junctions / metabolism*
  • Intercellular Junctions / ultrastructure
  • Kinesins
  • Membrane Glycoproteins / chemistry
  • Membrane Glycoproteins / genetics
  • Membrane Glycoproteins / metabolism
  • Mice
  • Microfilament Proteins / chemistry
  • Microfilament Proteins / metabolism*
  • Microscopy, Electron
  • Myocardium / chemistry
  • Myocardium / cytology
  • Myocardium / metabolism
  • Myosins
  • Nectins
  • Protein Structure, Tertiary
  • Rabbits
  • Receptors, Tumor Necrosis Factor*
  • Receptors, Tumor Necrosis Factor, Member 14
  • Receptors, Virus*
  • Vinculin / metabolism

Substances

  • AFDN protein, human
  • Afdn protein, mouse
  • Cadherins
  • Cell Adhesion Molecules
  • Membrane Glycoproteins
  • Microfilament Proteins
  • Nectins
  • Receptors, Tumor Necrosis Factor
  • Receptors, Tumor Necrosis Factor, Member 14
  • Receptors, Virus
  • TNFRSF14 protein, human
  • Tnfrsf14 protein, mouse
  • afadin
  • Vinculin
  • Myosins
  • Kinesins
  • Calcium