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Bacterial dynamin-like proteins reveal mechanism for membrane fusion

The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. While fission-specific proteins such as dynamin work as homo-oligomeric complexes, many fusion catalysts such as mitofusins or bacterial dynamin-like proteins (DLPs) act a...

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Autor principal: Bramkamp, Marc
Formato: Online Artículo Texto
Lenguaje:English
Publicado: Nature Publishing Group UK 2018
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162298/
https://www.ncbi.nlm.nih.gov/pubmed/30266939
http://dx.doi.org/10.1038/s41467-018-06559-6
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author Bramkamp, Marc
author_facet Bramkamp, Marc
author_sort Bramkamp, Marc
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description The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. While fission-specific proteins such as dynamin work as homo-oligomeric complexes, many fusion catalysts such as mitofusins or bacterial dynamin-like proteins (DLPs) act as hetero-oligomers. However, so far it was unclear how these hetero-oligomeric DLPs assemble and how they function in membrane remodeling. The group of Harry Low report now on the structure of a DLP pair from Campylobacter jejuni, allowing detailed insight into the assembly mechanism and membrane tethering activity.
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spelling pubmed-61622982018-10-01 Bacterial dynamin-like proteins reveal mechanism for membrane fusion Bramkamp, Marc Nat Commun Comment The dynamin superfamily of large GTPases comprises specialized members that catalyze fusion and fission of biological membranes. While fission-specific proteins such as dynamin work as homo-oligomeric complexes, many fusion catalysts such as mitofusins or bacterial dynamin-like proteins (DLPs) act as hetero-oligomers. However, so far it was unclear how these hetero-oligomeric DLPs assemble and how they function in membrane remodeling. The group of Harry Low report now on the structure of a DLP pair from Campylobacter jejuni, allowing detailed insight into the assembly mechanism and membrane tethering activity. Nature Publishing Group UK 2018-09-28 /pmc/articles/PMC6162298/ /pubmed/30266939 http://dx.doi.org/10.1038/s41467-018-06559-6 Text en © The Author(s) 2018 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 Comment
Bramkamp, Marc
Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title_full Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title_fullStr Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title_full_unstemmed Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title_short Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title_sort bacterial dynamin-like proteins reveal mechanism for membrane fusion
topic Comment
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6162298/
https://www.ncbi.nlm.nih.gov/pubmed/30266939
http://dx.doi.org/10.1038/s41467-018-06559-6
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