Bacterial dynamin-like proteins reveal mechanism for membrane fusion.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 30266939.
- Also identified by DOI 10.1038/s41467-018-06559-6 and PMC identifier 6162298.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
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.
Medical subject headings
- Bacterial Proteins
- Campylobacter jejuni
- Dynamins
- Membrane Fusion