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Dynein light chain interaction with the peroxisomal import docking complex modulates peroxisome biogenesis in yeast

Jinlan Chang1, Robert J Tower, David L Lancaster

  • 1Department of Cell Biology, University of Alberta, Edmonton, Alberta T6G 2H7, Canada.

Journal of Cell Science
|August 15, 2013
PubMed

Insights

The yeast protein Dyn2p is crucial for peroxisome assembly and function, impacting cell growth and protein import. Dyn2p works with the peroxisomal docking complex for optimal matrix protein import.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Biochemistry

Background:

  • Dynein is a motor complex involved in intracellular transport.
  • The dynein light chain, Dyn2p, was previously suggested to have a non-motor role in peroxisome biology.
  • Pex14p is a component of the peroxisomal matrix protein import docking complex.

Purpose of the Study:

  • To investigate the role of Dyn2p in peroxisome function and biogenesis in Yarrowia lipolytica.
  • To determine the relationship between Dyn2p and the peroxisomal matrix protein import machinery.

Main Methods:

  • Gene deletion studies in Yarrowia lipolytica.
  • Growth assays on oleic acid medium.
  • Microscopy to assess peroxisome morphology and protein localization.
  • Analysis of thiolase processing.
  • Co-immunoprecipitation and genetic interaction studies.

Main Results:

  • Yeast cells lacking Dyn2p showed impaired peroxisome function and biogenesis.
  • These cells exhibited poor growth on oleic acid, abnormal peroxisome morphology, and incorrect matrix protein localization.
  • The proteolytic processing of thiolase was absent in Dyn2p-deleted cells.
  • Dyn2p physically and genetically interacted with components of the peroxisomal docking complex, notably Pex17p.

Conclusions:

  • Dyn2p plays a significant role in the assembly of functional peroxisomes.
  • Dyn2p cooperates with the peroxisomal matrix protein import docking complex to ensure efficient matrix protein import.
  • These findings reveal a novel, motor-independent function for a dynein light chain in organelle biogenesis.
Keywords:
Docking complexDyneinOrganelle biogenesisPeroxinPeroxisomeYarrowia lipolytica

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