Mechanistic analysis of a dynamin effector

Laura L. Lackner, Jennifer S. Horner, Jodi Nunnari

Research output: Contribution to journalArticle

96 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)874-877
Number of pages4
JournalScience
Volume325
Issue number5942
DOIs
StatePublished - 2009

ASJC Scopus subject areas

  • General

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    Lackner, L. L., Horner, J. S., & Nunnari, J. (2009). Mechanistic analysis of a dynamin effector. Science, 325(5942), 874-877. https://doi.org/10.1126/science.1176921