Cell-cell junction formation: the role of Rap1 and Rap1 guanine nucleotide exchange factors

Biochim Biophys Acta. 2009 Apr;1788(4):790-6. doi: 10.1016/j.bbamem.2008.12.010. Epub 2008 Dec 29.

Abstract

Rap proteins are Ras-like small GTP-binding proteins that amongst others are involved in the control of cell-cell and cell-matrix adhesion. Several Rap guanine nucleotide exchange factors (RapGEFs) function to activate Rap. These multi-domain proteins, which include C3G, Epacs, PDZ-GEFs, RapGRPs and DOCK4, are regulated by various different stimuli and may function at different levels in junction formation. Downstream of Rap, a number of effector proteins have been implicated in junctional control, most notably the adaptor proteins AF6 and KRIT/CCM1. In this review, we will highlight the latest findings on the Rap signaling network in the control of epithelial and endothelial cell-cell junctions.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Adherens Junctions / physiology*
  • Animals
  • Endothelial Cells / ultrastructure
  • Guanine Nucleotide Exchange Factors / physiology*
  • Humans
  • Protein Structure, Tertiary
  • Signal Transduction / physiology*
  • Tight Junctions / physiology*
  • rap1 GTP-Binding Proteins / physiology*

Substances

  • Guanine Nucleotide Exchange Factors
  • RAPGEF3 protein, human
  • rap1 GTP-Binding Proteins