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Mechanistic analysis of a dynamin effector.

Science (New York, N.Y.) | Aug 14, 2009

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.

Pubmed ID: 19679814 RIS Download

Mesh terms: Adaptor Proteins, Signal Transducing | GTP Phosphohydrolases | Guanosine Triphosphate | Intracellular Membranes | Kinetics | Liposomes | Mitochondria | Mitochondrial Proteins | Models, Biological | Protein Binding | Protein Conformation | Protein Structure, Secondary | Saccharomyces cerevisiae Proteins

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Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM062942
  • Agency: NIGMS NIH HHS, Id: R01 GM097432
  • Agency: NIGMS NIH HHS, Id: 1F32GM078749
  • Agency: NIGMS NIH HHS, Id: R01GM062942

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