Journal
TRENDS IN CELL BIOLOGY
Volume 17, Issue 1, Pages 36-43Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2006.11.004
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Funding
- NATIONAL HEART, LUNG, AND BLOOD INSTITUTE [P01HL045100] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM029860] Funding Source: NIH RePORTER
- NHLBI NIH HHS [HL45100] Funding Source: Medline
- NIGMS NIH HHS [GM29860] Funding Source: Medline
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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 similar to 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.
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