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The mitochondrial fission receptor Mff selectively recruits oligomerized Drp1

Raymond Liu1, David C Chan2

  • 1Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA 91125.

Molecular Biology of the Cell
|October 9, 2015
PubMed

Insights

Dynamin-related protein 1 (Drp1) mediates mitochondrial fission. Its interaction with receptors like Mff is regulated by Drp1

Area of Science:

  • Cell biology
  • Molecular biology
  • Biochemistry

Background:

  • Dynamin-related protein 1 (Drp1) is a key GTPase regulating mitochondrial fission.
  • Drp1 functions through recruitment to the mitochondrial outer membrane by specific receptors.
  • Mitochondrial fission is crucial for cellular processes, and its dysregulation is linked to disease.

Purpose of the Study:

  • To investigate the molecular mechanisms governing the interaction between Drp1 and its receptor Mff.
  • To understand how Drp1 recruitment by different receptors (Mff, MiD49, MiD51) influences mitochondrial fission.
  • To elucidate the role of Drp1's insert B region in Mff-Drp1 complex formation.

Main Methods:

  • Genetic manipulation of Drp1 and its receptors.
  • Biochemical assays to study protein-protein interactions.
  • Analysis of Drp1 assembly states and their binding affinities.

Main Results:

  • The insert B region of Drp1 inhibits its interaction with Mff.
  • Drp1 mutants lacking insert B form stable complexes with Mff.
  • Mff selectively binds to higher-order Drp1 complexes, unlike MiD49 and MiD51 which bind Drp1 dimers.
  • Different Drp1 receptors may recruit distinct Drp1 subpopulations.

Conclusions:

  • Mff-mediated Drp1 recruitment differs from that of MiD49 and MiD51 due to distinct Drp1 binding preferences.
  • The insert B region of Drp1 is a critical negative regulator of Mff-Drp1 interactions.
  • Differential recruitment of Drp1 by its receptors contributes to the regulation of mitochondrial fission dynamics.

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