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Science. 2009 Aug 14;325(5942):874-7. doi: 10.1126/science.1176921.

Mechanistic analysis of a dynamin effector.

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  • 1Department of Molecular and Cellular Biology, University of California, Davis, CA 95616, USA.

Abstract

Dynamin-related proteins (DRPs) can generate forces to remodel membranes. In cells, DRPs require additional proteins [DRP-associated proteins (DAPs)] to conduct their functions. To dissect the mechanistic role of a DAP, we used the yeast mitochondrial division machine as a model, which requires the DRP Dnm1, and two other proteins, Mdv1 and Fis1. Mdv1 played a postmitochondrial targeting role in division by specifically interacting and coassembling with the guanosine triphosphate-bound form of Dnm1. This regulated interaction nucleated and promoted the self-assembly of Dnm1 into helical structures, which drive membrane scission. The nucleation of DRP assembly probably represents a general regulatory strategy for this family of filament-forming proteins, similar to F-actin regulation.

PMID:
19679814
[PubMed - indexed for MEDLINE]
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