Bacterial dynamin-like proteins reveal mechanism for membrane fusion

Abstract 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 (DL...

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Autor principal:	Marc Bramkamp
Formato:	article
Lenguaje:	EN
Publicado:	Nature Portfolio 2018
Materias:	Science Q
Acceso en línea:	https://doaj.org/article/89198d96cb944f12b960167adf3d578c
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spelling	oai:doaj.org-article:89198d96cb944f12b960167adf3d578c2021-12-02T14:38:53ZBacterial dynamin-like proteins reveal mechanism for membrane fusion10.1038/s41467-018-06559-62041-1723https://doaj.org/article/89198d96cb944f12b960167adf3d578c2018-09-01T00:00:00Zhttps://doi.org/10.1038/s41467-018-06559-6https://doaj.org/toc/2041-1723Abstract 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.Marc BramkampNature PortfolioarticleScienceQENNature Communications, Vol 9, Iss 1, Pp 1-3 (2018)
institution	DOAJ
collection	DOAJ
language	EN
topic	Science Q
spellingShingle	Science Q Marc Bramkamp Bacterial dynamin-like proteins reveal mechanism for membrane fusion
description	Abstract 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.
format	article
author	Marc Bramkamp
author_facet	Marc Bramkamp
author_sort	Marc Bramkamp
title	Bacterial dynamin-like proteins reveal mechanism for membrane fusion
title_short	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_sort	bacterial dynamin-like proteins reveal mechanism for membrane fusion
publisher	Nature Portfolio
publishDate	2018
url	https://doaj.org/article/89198d96cb944f12b960167adf3d578c
work_keys_str_mv	AT marcbramkamp bacterialdynaminlikeproteinsrevealmechanismformembranefusion
_version_	1718390847284707328

Bacterial dynamin-like proteins reveal mechanism for membrane fusion

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