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Ras GTPases’ interaction with effector domains: Breaking the families’ barrier

The Ras superfamily of proteins consists of five branches: Ras, Rho, Arf, Rab and Ran subfamilies. These proteins are involved in a plethora of biological functions spanning cytoskeletal organization, cell proliferation, transcription and intracellular trafficking. Ras-Binding Domains (RBDs) have cl...

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Detalles Bibliográficos
Autores principales: Patel, Manishha, Côté, Jean-François
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Landes Bioscience 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737747/
https://www.ncbi.nlm.nih.gov/pubmed/23986800
http://dx.doi.org/10.4161/cib.24298
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author Patel, Manishha
Côté, Jean-François
author_facet Patel, Manishha
Côté, Jean-François
author_sort Patel, Manishha
collection PubMed
description The Ras superfamily of proteins consists of five branches: Ras, Rho, Arf, Rab and Ran subfamilies. These proteins are involved in a plethora of biological functions spanning cytoskeletal organization, cell proliferation, transcription and intracellular trafficking. Ras-Binding Domains (RBDs) have classically been identified as autonomous ubiquitin-like folded regions that bind certain activated Ras GTPases of the Ras subfamily. In general, RBDs in many proteins have been tagged with membrane-targeting functions as in the case of the well-characterized c-Raf-RBD/Ras interaction. However, it is becoming apparent that the definition and functions of RBDs need to be revamped in order to reflect the new discoveries associated with this domain. Here, we discuss in more detail the recent advances associated with these RBDs. We highlight research identifying RBDs in formins, ELMOs and the RhoGEF, Syx and discuss the emerging role for RBDs in controlling autoinhibition relief and the newly recognized versatility of RBDs to interact with Rho and Arf family GTPases. In addition, these recent findings raise the exciting hypothesis that functional RBDs remain hidden in the proteome and are ready to be uncovered.
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spelling pubmed-37377472013-08-28 Ras GTPases’ interaction with effector domains: Breaking the families’ barrier Patel, Manishha Côté, Jean-François Commun Integr Biol Mini Review The Ras superfamily of proteins consists of five branches: Ras, Rho, Arf, Rab and Ran subfamilies. These proteins are involved in a plethora of biological functions spanning cytoskeletal organization, cell proliferation, transcription and intracellular trafficking. Ras-Binding Domains (RBDs) have classically been identified as autonomous ubiquitin-like folded regions that bind certain activated Ras GTPases of the Ras subfamily. In general, RBDs in many proteins have been tagged with membrane-targeting functions as in the case of the well-characterized c-Raf-RBD/Ras interaction. However, it is becoming apparent that the definition and functions of RBDs need to be revamped in order to reflect the new discoveries associated with this domain. Here, we discuss in more detail the recent advances associated with these RBDs. We highlight research identifying RBDs in formins, ELMOs and the RhoGEF, Syx and discuss the emerging role for RBDs in controlling autoinhibition relief and the newly recognized versatility of RBDs to interact with Rho and Arf family GTPases. In addition, these recent findings raise the exciting hypothesis that functional RBDs remain hidden in the proteome and are ready to be uncovered. Landes Bioscience 2013-07-01 2013-04-22 /pmc/articles/PMC3737747/ /pubmed/23986800 http://dx.doi.org/10.4161/cib.24298 Text en Copyright © 2013 Landes Bioscience http://creativecommons.org/licenses/by-nc/3.0/ This is an open-access article licensed under a Creative Commons Attribution-NonCommercial 3.0 Unported License. The article may be redistributed, reproduced, and reused for non-commercial purposes, provided the original source is properly cited.
spellingShingle Mini Review
Patel, Manishha
Côté, Jean-François
Ras GTPases’ interaction with effector domains: Breaking the families’ barrier
title Ras GTPases’ interaction with effector domains: Breaking the families’ barrier
title_full Ras GTPases’ interaction with effector domains: Breaking the families’ barrier
title_fullStr Ras GTPases’ interaction with effector domains: Breaking the families’ barrier
title_full_unstemmed Ras GTPases’ interaction with effector domains: Breaking the families’ barrier
title_short Ras GTPases’ interaction with effector domains: Breaking the families’ barrier
title_sort ras gtpases’ interaction with effector domains: breaking the families’ barrier
topic Mini Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3737747/
https://www.ncbi.nlm.nih.gov/pubmed/23986800
http://dx.doi.org/10.4161/cib.24298
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