Lumenal peroxisomal protein aggregates are removed by concerted fission and autophagy events

Selvambigai Manivannan, Rinse de Boer, Marten Veenhuis, Ida J. van der Klei*

*Corresponding author for this work

Research output: Contribution to journalArticleAcademicpeer-review

24 Citations (Scopus)

Abstract

We demonstrated that in the yeast Hansenula polymorpha peroxisome fission and degradation are coupled processes that are important to remove intra-organellar protein aggregates. Protein aggregates were formed in peroxisomes upon synthesis of a mutant catalase variant. We showed that the introduction of these aggregates in the peroxisomal lumen had physiological disadvantages as it affected growth and caused enhanced levels of reactive oxygen species. Formation of the protein aggregates was followed by asymmetric peroxisome fission to separate the aggregate from the mother organelle. Subsequently, these small, protein aggregate-containing organelles were degraded by autophagy. In line with this observation we showed that the degradation of the protein aggregates was strongly reduced in dnm1 and pex11 cells in which peroxisome fission is reduced. Moreover, this process was dependent on Atg1 and Atg11.

Original languageEnglish
Pages (from-to)1044-1056
Number of pages13
JournalAutophagy
Volume9
Issue number7
DOIs
Publication statusPublished - 1-Jul-2013

Keywords

  • yeast
  • peroxisome
  • protein aggregate
  • fission
  • autophagy
  • YEAST HANSENULA-POLYMORPHA
  • SACCHAROMYCES-CEREVISIAE
  • SELECTIVE INACTIVATION
  • ENDOPLASMIC-RETICULUM
  • DEGRADATION
  • GENE
  • MEMBRANE
  • REQUIRES
  • MACROPEXOPHAGY
  • PROTEOSTASIS

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