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Interchangeable adaptors regulate mitochondrial dynamin assembly for membrane scission

Sajjan Koirala1, Qian Guo, Raghav Kalia

  • 1Department of Biochemistry, University of Utah School of Medicine, Salt Lake City, UT 84112, USA.

Proceedings of the National Academy of Sciences of the United States of America
|March 27, 2013
PubMed

Insights

Mitochondrial fission relies on dynamin GTPases and adaptor proteins. Researchers found that specific adaptors, like MiDs, can alter dynamin structure, aiding in mitochondrial division.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Mitochondrial fission is crucial for cellular function and is mediated by dynamin-related GTPases (Dnm1/Drp1) and adaptor proteins.
  • Adaptor proteins (Fis1, Mdv1, Mff, MiDs) are known to recruit GTPases to the mitochondrial surface, but their role in membrane scission is unclear.

Purpose of the Study:

  • To determine the minimal combinations of GTPases and adaptors sufficient for mitochondrial fission.
  • To investigate the role of adaptor proteins in both GTPase recruitment and membrane scission.

Main Methods:

  • Utilized a yeast strain deficient in all known fission proteins.
  • Assessed mitochondrial fission using minimal combinations of GTPases and adaptors.
  • Performed in vitro co-assembly assays with Drp1 and MiDs.

Main Results:

  • Fis1 is dispensable for mitochondrial fission.
  • Membrane-anchored Mdv1, Mff, or MiDs, when paired with their respective GTPases, are sufficient for mitochondrial division.
  • MiDs coassemble with Drp1 in vitro, forming a heteropolymer with a narrower diameter than Drp1 homopolymers.

Conclusions:

  • Specific adaptor proteins, such as MiDs, are sufficient to mediate mitochondrial fission.
  • Adaptor proteins can directly alter the structural architecture of dynamin GTPase polymers.
  • This structural alteration by adaptors likely facilitates mitochondrial membrane constriction and scission.

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