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J Cell Sci. 2013 Oct 15;126(Pt 20):4698-706. doi: 10.1242/jcs.129056. Epub 2013 Aug 13.

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

Author information

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

Abstract

Dynein is a large macromolecular motor complex that moves cargo along microtubules. A motor-independent role for the light chain of dynein, Dyn2p, in peroxisome biology in Saccharomyces cerevisiae was suggested from its interaction with Pex14p, a component of the peroxisomal matrix protein import docking complex. Here we show that cells of the yeast Yarrowia lipolytica deleted for the gene encoding the homologue of Dyn2p are impaired in peroxisome function and biogenesis. These cells exhibit compromised growth on medium containing oleic acid as the carbon source, the metabolism of which requires functional peroxisomes. Their peroxisomes have abnormal morphology, atypical matrix protein localization, and an absence of proteolytic processing of the matrix enzyme thiolase, which normally occurs upon its import into the peroxisome. We also show physical and genetic interactions between Dyn2p and members of the docking complex, particularly Pex17p. Together, our results demonstrate a role for Dyn2p in the assembly of functional peroxisomes and provide evidence that Dyn2p acts in cooperation with the peroxisomal matrix protein import docking complex to effect optimal matrix protein import.

KEYWORDS:

Docking complex; Dynein; Organelle biogenesis; Peroxin; Peroxisome; Yarrowia lipolytica

PMID:
23943868
[PubMed - indexed for MEDLINE]
PMCID:
PMC3795339
Free PMC Article
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