2016-06-15
AUTHORSRichard G. Hodge, Anne J. Ridley
ABSTRACTKey PointsRho GTPases regulate a wide range of cellular responses, including changes to the cytoskeleton and cell adhesion. Their activity therefore needs to be precisely controlled to determine which response occurs, depending on the context and stimulus.Most Rho GTPases cycle between an active GTP-bound and an inactive GDP-bound form, a process that is regulated by guanine nucleotide exchange factors (GEFs), GTPase-activating proteins (GAPs) and guanine nucleotide dissociation inhibitors (GDIs). In their GTP-bound form, they interact with a diverse range of different targets to induce cellular responses.In addition to GTP–GDP cycling, Rho GTPases are regulated by a diverse range of post-translational modifications, including phosphorylation, ubiquitylation and sumoylation, which alter their localization, activity and stability.GEFs, GAPs and GDIs are also regulated by post-translational modifications, which in turn affect their activity, stability and ability to form protein complexes. These changes then impinge on where and when Rho GTPases are activated.The spatiotemporal activation of Rho GTPases is coordinated by a complex network of post-translational modifications and protein–protein interactions. This determines which Rho GTPase targets are activated, and hence the cellular outcome. More... »
PAGES496-510
http://scigraph.springernature.com/pub.10.1038/nrm.2016.67
DOIhttp://dx.doi.org/10.1038/nrm.2016.67
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PUBMEDhttps://www.ncbi.nlm.nih.gov/pubmed/27301673
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