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Structural Basis of Membrane Trafficking by Rab Family Small G Protein

The Ras-superfamily of small G proteins is a family of GTP hydrolases that is regulated by GTP/GDP binding states. One member of the Ras-superfamily, Rab, is involved in the regulation of vesicle trafficking, which is critical to endocytosis, biosynthesis, secretion, cell differentiation and cell gr...

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Autor principal: Park, Hyun Ho
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Molecular Diversity Preservation International (MDPI) 2013
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676764/
https://www.ncbi.nlm.nih.gov/pubmed/23698755
http://dx.doi.org/10.3390/ijms14058912
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author Park, Hyun Ho
author_facet Park, Hyun Ho
author_sort Park, Hyun Ho
collection PubMed
description The Ras-superfamily of small G proteins is a family of GTP hydrolases that is regulated by GTP/GDP binding states. One member of the Ras-superfamily, Rab, is involved in the regulation of vesicle trafficking, which is critical to endocytosis, biosynthesis, secretion, cell differentiation and cell growth. The active form of the Rab proteins, which contains GTP, can recruit specific binding partners, such as sorting adaptors, tethering factors, kinases, phosphatases and motor proteins, thereby influencing vesicle formation, transport, and tethering. Many Rab proteins share the same interacting partners and perform unique roles in specific locations. Because functional loss of the Rab pathways has been implicated in a variety of diseases, the Rab GTPase family has been extensively investigated. In this review, we summarize Rab GTPase- mediated membrane trafficking while focusing on the structures of Rab protein and Rab-effector complexes. This review provides detailed information that helps explain how the Rab GTPase family is involved in membrane trafficking.
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spelling pubmed-36767642013-07-02 Structural Basis of Membrane Trafficking by Rab Family Small G Protein Park, Hyun Ho Int J Mol Sci Review The Ras-superfamily of small G proteins is a family of GTP hydrolases that is regulated by GTP/GDP binding states. One member of the Ras-superfamily, Rab, is involved in the regulation of vesicle trafficking, which is critical to endocytosis, biosynthesis, secretion, cell differentiation and cell growth. The active form of the Rab proteins, which contains GTP, can recruit specific binding partners, such as sorting adaptors, tethering factors, kinases, phosphatases and motor proteins, thereby influencing vesicle formation, transport, and tethering. Many Rab proteins share the same interacting partners and perform unique roles in specific locations. Because functional loss of the Rab pathways has been implicated in a variety of diseases, the Rab GTPase family has been extensively investigated. In this review, we summarize Rab GTPase- mediated membrane trafficking while focusing on the structures of Rab protein and Rab-effector complexes. This review provides detailed information that helps explain how the Rab GTPase family is involved in membrane trafficking. Molecular Diversity Preservation International (MDPI) 2013-04-25 /pmc/articles/PMC3676764/ /pubmed/23698755 http://dx.doi.org/10.3390/ijms14058912 Text en © 2013 by the authors; licensee MDPI, Basel, Switzerland http://creativecommons.org/licenses/by/3.0 This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Review
Park, Hyun Ho
Structural Basis of Membrane Trafficking by Rab Family Small G Protein
title Structural Basis of Membrane Trafficking by Rab Family Small G Protein
title_full Structural Basis of Membrane Trafficking by Rab Family Small G Protein
title_fullStr Structural Basis of Membrane Trafficking by Rab Family Small G Protein
title_full_unstemmed Structural Basis of Membrane Trafficking by Rab Family Small G Protein
title_short Structural Basis of Membrane Trafficking by Rab Family Small G Protein
title_sort structural basis of membrane trafficking by rab family small g protein
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3676764/
https://www.ncbi.nlm.nih.gov/pubmed/23698755
http://dx.doi.org/10.3390/ijms14058912
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