Bacterial dynamin-like proteins reveal mechanism for membrane fusion

Marc Bramkamp ()
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Marc Bramkamp: Ludwig-Maximilians-Universität München

Nature Communications, 2018, vol. 9, issue 1, 1-3

Abstract: 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.

Date: 2018
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DOI: 10.1038/s41467-018-06559-6

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