p190RhoGAP proteins contain pseudoGTPase domains

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...

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Autores principales: Stiegler, Amy L., Boggon, Titus J.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2017
Materias:
Article
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593906/
https://www.ncbi.nlm.nih.gov/pubmed/28894085
http://dx.doi.org/10.1038/s41467-017-00483-x
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author Stiegler, Amy L.
Boggon, Titus J.
author_facet Stiegler, Amy L.
Boggon, Titus J.
author_sort Stiegler, Amy L.
collection PubMed
description 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.
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spelling pubmed-55939062017-09-13 p190RhoGAP proteins contain pseudoGTPase domains Stiegler, Amy L. Boggon, Titus J. Nat Commun Article 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. Nature Publishing Group UK 2017-09-11 /pmc/articles/PMC5593906/ /pubmed/28894085 http://dx.doi.org/10.1038/s41467-017-00483-x Text en © The Author(s) 2017 Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.
spellingShingle Article
Stiegler, Amy L.
Boggon, Titus J.
p190RhoGAP proteins contain pseudoGTPase domains
title p190RhoGAP proteins contain pseudoGTPase domains
title_full p190RhoGAP proteins contain pseudoGTPase domains
title_fullStr p190RhoGAP proteins contain pseudoGTPase domains
title_full_unstemmed p190RhoGAP proteins contain pseudoGTPase domains
title_short p190RhoGAP proteins contain pseudoGTPase domains
title_sort p190rhogap proteins contain pseudogtpase domains
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5593906/
https://www.ncbi.nlm.nih.gov/pubmed/28894085
http://dx.doi.org/10.1038/s41467-017-00483-x
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