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p190RhoGAP proteins contain pseudoGTPase domains

Author

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  • Amy L. Stiegler

    (Yale University School of Medicine)

  • Titus J. Boggon

    (Yale University School of Medicine
    Yale University School of Medicine
    Yale University School of Medicine)

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.

Suggested Citation

  • Amy L. Stiegler & Titus J. Boggon, 2017. "p190RhoGAP proteins contain pseudoGTPase domains," Nature Communications, Nature, vol. 8(1), pages 1-9, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-00483-x
    DOI: 10.1038/s41467-017-00483-x
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