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MIEF1/2 function as adaptors to recruit Drp1 to mitochondria and regulate the association of Drp1 with Mff

Rong Yu1, Tong Liu1, Shao-Bo Jin2

  • 1Department of Oncology-Pathology, Karolinska Institutet, CCK R8:05, Karolinska University Hospital Solna, SE-171 76, Stockholm, Sweden.

Scientific Reports
|April 15, 2017
PubMed

Insights

Mitochondrial fission relies on Drp1 recruitment, mediated by Mff and MIEF1/2 receptors. MIEFs act as adaptors, linking Drp1 and Mff to control fission, with MIEF levels balancing mitochondrial dynamics.

Area of Science:

  • Cell Biology
  • Mitochondrial Biology
  • Molecular Cell Biology

Background:

  • Mitochondrial dynamics, crucial for cellular function, involves fission and fusion.
  • Drp1 recruitment to mitochondria is essential for mitochondrial fission.
  • Mff and MIEF1/2 (MiD51/49) are known receptors for Drp1, but their collaborative roles are unclear.

Purpose of the Study:

  • To elucidate the cooperative mechanisms of Mff and MIEF1/2 in Drp1-mediated mitochondrial fission.
  • To investigate the role of MIEFs as adaptors linking Drp1 and Mff.

Main Methods:

  • Co-immunoprecipitation assays to detect protein interactions.
  • Mitochondrial morphology analysis in cells with altered MIEF expression.
  • Western blotting to assess protein levels and recruitment.

Main Results:

  • MIEFs form a trimeric complex with Drp1 and Mff on the mitochondrial surface.
  • MIEFs act as adaptors, linking Drp1 and Mff, and regulating Drp1 accumulation.
  • Loss of MIEFs impairs Drp1-Mff interactions and Mff-induced Drp1 recruitment.
  • MIEF levels dictate mitochondrial morphology: high levels cause elongation, while moderate levels promote fission.

Conclusions:

  • MIEFs and Mff function coordinately in Drp1-mediated mitochondrial fission.
  • The relative levels of MIEF1/2 and Mff determine the balance between mitochondrial fission and fusion.

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