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The crystal structure of dynamin

Author

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  • Marijn G. J. Ford

    (University of California, Davis, Davis, California 95616, USA)

  • Simon Jenni

    (Harvard Medical School)

  • Jodi Nunnari

    (University of California, Davis, Davis, California 95616, USA)

Abstract

Dynamin-related proteins (DRPs) are multi-domain GTPases that function via oligomerization and GTP-dependent conformational changes to play central roles in regulating membrane structure across phylogenetic kingdoms. How DRPs harness self-assembly and GTP-dependent conformational changes to remodel membranes is not understood. Here we present the crystal structure of an assembly-deficient mammalian endocytic DRP, dynamin 1, lacking the proline-rich domain, in its nucleotide-free state. The dynamin 1 monomer is an extended structure with the GTPase domain and bundle signalling element positioned on top of a long helical stalk with the pleckstrin homology domain flexibly attached on its opposing end. Dynamin 1 dimer and higher order dimer multimers form via interfaces located in the stalk. Analysis of these interfaces provides insight into DRP family member specificity and regulation and provides a framework for understanding the biogenesis of higher order DRP structures and the mechanism of DRP-mediated membrane scission events.

Suggested Citation

  • Marijn G. J. Ford & Simon Jenni & Jodi Nunnari, 2011. "The crystal structure of dynamin," Nature, Nature, vol. 477(7366), pages 561-566, September.
    • Handle: RePEc:nat:nature:v:477:y:2011:i:7366:d:10.1038_nature10441
    DOI: 10.1038/nature10441
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    Cited by:

    1. Kristy Rochon & Brianna L. Bauer & Nathaniel A. Roethler & Yuli Buckley & Chih-Chia Su & Wei Huang & Rajesh Ramachandran & Maria S. K. Stoll & Edward W. Yu & Derek J. Taylor & Jason A. Mears, 2024. "Structural basis for regulated assembly of the mitochondrial fission GTPase Drp1," Nature Communications, Nature, vol. 15(1), pages 1-10, December.

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