Catching a GEF by its tail.

Rafael García-Mata; Keith Burridge

doi:10.1016/j.tcb.2006.11.004

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PubMed · 17126549

Catching a GEF by its tail.

Rafael García-Mata·Keith Burridge

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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.

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Alternative Splicing Amino Acid Motifs Animals Humans Models, Biological Phosphorylation Protein Binding Protein Isoforms Protein Structure, Tertiary Proteins Signal Transduction rho GTP-Binding Proteins Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Review

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Rafael García-Mata, Keith Burridge. 2006-11-28. Catching a GEF by its tail.. https://doi.org/10.1016/j.tcb.2006.11.004

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