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Dnm1p-dependent peroxisome fission requires Caf4p, Mdv1p and Fis1p

Alison M Motley1, Gemma P Ward, Ewald H Hettema

  • 1Department of Molecular Biology and Biotechnology, University of Sheffield, Firth Court, Western Bank, Sheffield, S10 2TN, UK.

Journal of Cell Science
|May 1, 2008
PubMed

Insights

Yeast peroxisome fission involves two distinct protein machineries. Dnm1p-dependent fission requires Fis1p, Caf4p, and Mdv1p, while Vps1p-dependent fission operates independently.

Area of Science:

  • Cell Biology
  • Organelle Biogenesis

Background:

  • Yeast peroxisomes multiply through a process called fission.
  • This process relies on two key dynamin-related proteins: Dnm1p and Vps1p.

Purpose of the Study:

  • To elucidate the distinct molecular mechanisms and protein requirements for Dnm1p- and Vps1p-dependent peroxisome fission.
  • To investigate the interplay between Dnm1p, Vps1p, and associated factors in peroxisome division.

Main Methods:

  • Utilized an in vivo fission assay to analyze peroxisome division in yeast.
  • Employed fluorescence microscopy to track the localization of GFP-tagged proteins (Caf4p, Mdv1p) in relation to peroxisomes.
  • Investigated the effects of protein overexpression on fission defects.

Main Results:

  • Dnm1p-dependent peroxisome fission requires the proteins Fis1p, Caf4p, and Mdv1p.
  • The association of Caf4p and Mdv1p with peroxisomes is dependent on Fis1p.
  • Vps1p-dependent peroxisome fission occurs independently of Fis1p, Caf4p, and Mdv1p.
  • Vps1p plays a more significant role in peroxisome fission when yeast is grown on glucose.
  • Dnm1p and Vps1p function in separate fission machineries, as evidenced by non-reciprocal rescue experiments.

Conclusions:

  • Yeast peroxisome fission is executed by two independent protein machineries involving Dnm1p and Vps1p.
  • Dnm1p-mediated peroxisome proliferation may be linked to mitochondrial dysfunction, suggesting a role in coordinating organelle biogenesis.

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