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The mechanoenzymatic core of dynamin-related protein 1 comprises the minimal machinery required for membrane

Christopher A Francy1, Frances J D Alvarez1, Louie Zhou1

  • 1From the Department of Pharmacology, Center for Mitochondrial Diseases, and Cleveland Center for Membrane and Structural Biology, and.

The Journal of Biological Chemistry
|March 15, 2015
PubMed

Insights

Dynamin-related protein 1 (Drp1) constricts lipid bilayers via GTP hydrolysis. Its variable domain regulates assembly and membrane curvature, while the core alone mediates constriction.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitochondria are vital organelles undergoing fission and fusion.
  • Dynamin-related protein 1 (Drp1) is key to mitochondrial fission.
  • Drp1's structure includes a mechanochemical core and a variable domain of unknown function.

Purpose of the Study:

  • To elucidate the mechanism of Drp1-mediated membrane constriction.
  • To determine the role of Drp1's variable domain in its function.
  • To investigate the necessity of the variable domain for Drp1's membrane activity.

Main Methods:

  • Time-resolved electron microscopy (EM).
  • Rigorous statistical analyses.
  • Biochemical assays of Drp1 activity.

Main Results:

  • Full-length Drp1 constricts lipid bilayers through a GTP hydrolysis-dependent mechanism.
  • The variable domain of Drp1 limits premature assembly and promotes membrane curvature.
  • The Drp1 mechanochemical core, without the variable domain, can independently mediate GTP hydrolysis-dependent membrane constriction.

Conclusions:

  • Drp1 utilizes GTP hydrolysis for membrane constriction.
  • The variable domain plays a regulatory role in Drp1 assembly and membrane interaction.
  • The core mechanochemical domain is sufficient for the fundamental membrane constric tion activity of Drp1.
Keywords:
DynaminDynamin-related Protein 1Electron Microscopy (EM)GTPaseMitochondriaMitochondrial FissionProtein Conformational ChangesProtein Self-assembly

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