p190RhoGAP proteins contain pseudoGTPase domains

Amy L. Stiegler and Titus J. Boggon ()
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Amy L. Stiegler: Yale University School of Medicine
Titus J. Boggon: Yale University School of Medicine

Nature Communications, 2017, vol. 8, issue 1, 1-9

Abstract: Abstract The two p190RhoGAP proteins, p190RhoGAP-A and -B, are key regulators of Rho GTPase signaling and are essential for actin cytoskeletal structure and contractility. Here we report the discovery of two evolutionarily conserved GTPase-like domains located in the ‘middle domain’, previously thought to be unstructured. Deletion of these domains reduces RhoGAP activity. Crystal structures, MANT-GTPγS binding, thermal denaturation, biochemical assays and sequence homology analysis all strongly support defects in nucleotide-binding activity. Analysis of p190RhoGAP proteins therefore indicates the presence of two previously unidentified domains which represent an emerging group of pseudoenzymes, the pseudoGTPases.

Date: 2017
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DOI: 10.1038/s41467-017-00483-x

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