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TitleThe Structure of the Drp1 Lattice on Membrane.
Journal, issue, pagesJ Mol Biol, Vol. 437, Issue 12, Page 169125, Year 2025
Publish dateApr 2, 2025
AuthorsRuizhi Peng / Kristy Rochon / Anelise N Hutson / Scott M Stagg / Jason A Mears /
PubMed AbstractMitochondrial health relies on the membrane fission mediated by dynamin-related protein 1 (Drp1). Previous structural studies of Drp1 on remodeled membranes were hampered by heterogeneity, leaving a ...Mitochondrial health relies on the membrane fission mediated by dynamin-related protein 1 (Drp1). Previous structural studies of Drp1 on remodeled membranes were hampered by heterogeneity, leaving a critical gap in the understanding of the mitochondrial fission mechanisms. Here we present a cryo-electron microscopy structure of full-length human Drp1 decorated on membrane tubules. Using the reconstruction of average subtracted tubular regions (RASTR) technique, we report that Drp1 forms a locally ordered lattice along the tubule without global helical symmetry. The filaments in the lattice are similar to dynamin rungs with conserved stalk interactions. Adjacent filaments are connected by GTPase domain interactions in a novel stacked conformation. We identified two states of the Drp1 lattice among the heterogenous dataset representing conformational changes around hinge 1. Additionally, we observed contact between Drp1 and membrane that can be assigned to the variable domain sequence. Together these structures revealed a putative mechanism by which Drp1 constricts mitochondria membranes in a stepwise, "ratchet" manner.
External linksJ Mol Biol / PubMed:40185198 / PubMed Central
MethodsEM (single particle)
Resolution14.73 Å
Structure data

43045

8v8t

EMDB-43045, PDB-8v8t:
Asymmetrical subunit from a Drp1 lattice on PA nanotubes
Method: EM (single particle) / Resolution: 14.73 Å

Source
  • homo sapiens (human)
KeywordsHYDROLASE / membrane remodeling GTPase

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