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Recent insights into the structure and function of Mitofusins in mitochondrial fusion

Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include,...

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Detalles Bibliográficos
Autores principales: Cohen, Mickael M, Tareste, David
Formato: Online Artículo Texto
Lenguaje:English
Publicado: F1000 Research Limited 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6317495/
https://www.ncbi.nlm.nih.gov/pubmed/30647902
http://dx.doi.org/10.12688/f1000research.16629.1
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author Cohen, Mickael M
Tareste, David
author_facet Cohen, Mickael M
Tareste, David
author_sort Cohen, Mickael M
collection PubMed
description Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include, in addition to their GTPase and transmembrane domains, two heptad repeat domains, HR1 and HR2. All four regions are crucial for Mitofusin function, but their precise contribution to mitochondrial docking and fusion events has remained elusive until very recently. In this commentary, we first give an overview of the established strategies employed by various protein machineries distinct from Mitofusins to mediate membrane fusion. We then present recent structure–function data on Mitofusins that provide important novel insights into their mode of action in mitochondrial fusion.
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spelling pubmed-63174952019-01-14 Recent insights into the structure and function of Mitofusins in mitochondrial fusion Cohen, Mickael M Tareste, David F1000Res Review Mitochondria undergo frequent fusion and fission events to adapt their morphology to cellular needs. Homotypic docking and fusion of outer mitochondrial membranes are controlled by Mitofusins, a set of large membrane-anchored GTPase proteins belonging to the dynamin superfamily. Mitofusins include, in addition to their GTPase and transmembrane domains, two heptad repeat domains, HR1 and HR2. All four regions are crucial for Mitofusin function, but their precise contribution to mitochondrial docking and fusion events has remained elusive until very recently. In this commentary, we first give an overview of the established strategies employed by various protein machineries distinct from Mitofusins to mediate membrane fusion. We then present recent structure–function data on Mitofusins that provide important novel insights into their mode of action in mitochondrial fusion. F1000 Research Limited 2018-12-28 /pmc/articles/PMC6317495/ /pubmed/30647902 http://dx.doi.org/10.12688/f1000research.16629.1 Text en Copyright: © 2018 Cohen MM and Tareste D http://creativecommons.org/licenses/by/4.0/ This is an open access article distributed under the terms of the Creative Commons Attribution Licence, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Review
Cohen, Mickael M
Tareste, David
Recent insights into the structure and function of Mitofusins in mitochondrial fusion
title Recent insights into the structure and function of Mitofusins in mitochondrial fusion
title_full Recent insights into the structure and function of Mitofusins in mitochondrial fusion
title_fullStr Recent insights into the structure and function of Mitofusins in mitochondrial fusion
title_full_unstemmed Recent insights into the structure and function of Mitofusins in mitochondrial fusion
title_short Recent insights into the structure and function of Mitofusins in mitochondrial fusion
title_sort recent insights into the structure and function of mitofusins in mitochondrial fusion
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6317495/
https://www.ncbi.nlm.nih.gov/pubmed/30647902
http://dx.doi.org/10.12688/f1000research.16629.1
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