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Mechanistic analysis of a dynamin effector.

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

Authors

  • Lackner LL
  • Horner JS
  • Nunnari J

Journal

Science (New York, N.Y.)

Publication Data

August 14, 2009

Associated Grants

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

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