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Trends Cell Biol. 2007 Jan;17(1):36-43. Epub 2006 Nov 28.

Catching a GEF by its tail.

Author information

1
Department of Cell and Developmental Biology and Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, 12-026 Lineberger, CB#7295, Chapel Hill, NC 27599, USA. rafaelgm@med.unc.edu <rafaelgm@med.unc.edu>

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.

PMID:
17126549
DOI:
10.1016/j.tcb.2006.11.004
[Indexed for MEDLINE]

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