Catching a GEF by its tail

Trends Cell Biol. 2007 Jan;17(1):36-43. doi: 10.1016/j.tcb.2006.11.004. Epub 2006 Nov 28.

Abstract

The activation of Rho GTPases is mediated by guanine-nucleotide exchange factors (GEFs), which catalyze the exchange of GDP for GTP. Rho-GEFs are a very diverse family, with >70 members in humans. Bioinformatics analysis of the human Rho-GEFs shows that approximately 40% contain a putative PDZ-binding motif at the C-terminus. PDZ domains are protein-protein interaction domains that act as scaffolds to concentrate signaling molecules at specialized regions in the cell. We propose that the interaction between Rho-GEFs and PDZ-domain proteins is a general mechanism that controls Rho-GEF targeting and activation, helping to restrict and concentrate the exchange activity to appropriate subcellular destinations. Here, we summarize recent data that highlight the importance of these interactions in Rho-GEF regulation.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Alternative Splicing
  • Amino Acid Motifs
  • Animals
  • Humans
  • Models, Biological
  • Phosphorylation
  • Protein Binding
  • Protein Isoforms
  • Protein Structure, Tertiary
  • Proteins / chemistry
  • Signal Transduction
  • rho GTP-Binding Proteins / chemistry*
  • rho GTP-Binding Proteins / physiology

Substances

  • Protein Isoforms
  • Proteins
  • rho GTP-Binding Proteins