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Updated: Jun 28, 2025

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The Structure of the Drp1 Lattice on Membrane

Ruizhi Peng1, Kristy Rochon2, Anelise N Hutson2

  • 1Institute of Molecular Biophysics, Florida State University, Tallahassee, Florida, USA.

Biorxiv : the Preprint Server for Biology
|April 15, 2024
PubMed

Insights

Dynamin-related protein 1 (Drp1) structures reveal a novel mechanism for mitochondrial membrane fission. Drp1 forms a lattice on tubules, constricting membranes in a stepwise "ratchet" manner for mitochondrial health.

Area of Science:

  • Cell Biology
  • Structural Biology
  • Biochemistry

Background:

  • Mitochondrial health depends on membrane dynamics, particularly fission.
  • Dynamin-related protein 1 (Drp1) is crucial for mitochondrial fission.
  • Previous structural data on Drp1 on membranes were limited by heterogeneity.

Purpose of the Study:

  • To determine the structure of full-length human Drp1 on membrane tubules.
  • To elucidate the mechanism of mitochondrial membrane fission mediated by Drp1.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of human Drp1 on membrane tubules.
  • Reconstruction of average subtracted tubular regions (RASTR) technique.
  • Analysis of Drp1 lattice formation and conformational states.

Main Results:

  • Drp1 forms a locally ordered lattice on membrane tubules, lacking global helical symmetry.
  • The Drp1 lattice exhibits conserved dynamin rung-like interactions and novel stacked GTPase domain conformations.
  • Two distinct Drp1 lattice states were identified, indicating conformational changes.
  • Drp1-membrane contacts were observed, linked to its variable domain.

Conclusions:

  • The Drp1 lattice structure provides insights into mitochondrial fission.
  • A stepwise,

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