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Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors
The 20 members of the Rho GTPase family are key regulators of a wide-variety of biological activities. In response to activation, they signal via downstream effector proteins to induce dynamic alterations in the organization of the actomyosin cytoskeleton. In this review, post-translational modifica...
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Taylor & Francis
2016
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5927519/ https://www.ncbi.nlm.nih.gov/pubmed/27548350 http://dx.doi.org/10.1080/21541248.2016.1218407 |
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author | Olson, Michael F. |
author_facet | Olson, Michael F. |
author_sort | Olson, Michael F. |
collection | PubMed |
description | The 20 members of the Rho GTPase family are key regulators of a wide-variety of biological activities. In response to activation, they signal via downstream effector proteins to induce dynamic alterations in the organization of the actomyosin cytoskeleton. In this review, post-translational modifications, mechanisms of dysregulation identified in human pathological conditions, and the ways that Rho GTPases might be targeted for chemotherapy will be discussed. |
format | Online Article Text |
id | pubmed-5927519 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Taylor & Francis |
record_format | MEDLINE/PubMed |
spelling | pubmed-59275192018-05-02 Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors Olson, Michael F. Small GTPases Reviews The 20 members of the Rho GTPase family are key regulators of a wide-variety of biological activities. In response to activation, they signal via downstream effector proteins to induce dynamic alterations in the organization of the actomyosin cytoskeleton. In this review, post-translational modifications, mechanisms of dysregulation identified in human pathological conditions, and the ways that Rho GTPases might be targeted for chemotherapy will be discussed. Taylor & Francis 2016-08-22 /pmc/articles/PMC5927519/ /pubmed/27548350 http://dx.doi.org/10.1080/21541248.2016.1218407 Text en © 2016 The Author. Published with license by Taylor & Francis Group, LLC http://creativecommons.org/licenses/by-nc/3.0/ This is an Open Access article distributed under the terms of the Creative Commons Attribution-Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0/), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. The moral rights of the named author(s) have been asserted. |
spellingShingle | Reviews Olson, Michael F. Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
title | Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
title_full | Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
title_fullStr | Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
title_full_unstemmed | Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
title_short | Rho GTPases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
title_sort | rho gtpases, their post-translational modifications, disease-associated mutations and pharmacological inhibitors |
topic | Reviews |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5927519/ https://www.ncbi.nlm.nih.gov/pubmed/27548350 http://dx.doi.org/10.1080/21541248.2016.1218407 |
work_keys_str_mv | AT olsonmichaelf rhogtpasestheirposttranslationalmodificationsdiseaseassociatedmutationsandpharmacologicalinhibitors |