Uniqueness of the mechanism of protein import into the peroxisome matrix: Transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors

Sébastien Léon, Joel M. Goodman, Suresh Subramani

Research output: Contribution to journalReview articlepeer-review

87 Scopus citations

Abstract

Based on earlier suggestions that peroxisomes may have arisen from endosymbionts that later lost their DNA, it was expected that protein transport into this organelle would have parallels to systems found in other organelles of endosymbiont origin, such as mitochondria and chloroplasts. This review highlights three features of peroxisomal matrix protein import that make it unique in comparison with these other subcellular compartments - the ability of this organelle to transport folded, co-factor-bound and oligomeric proteins, the dynamics of the import receptors during the matrix protein import cycle and the existence of a peroxisomal quality-control pathway, which insures that the peroxisome membrane is cleared of cargo-free receptors.

Original languageEnglish (US)
Pages (from-to)1552-1564
Number of pages13
JournalBiochimica et Biophysica Acta - Molecular Cell Research
Volume1763
Issue number12
DOIs
StatePublished - Dec 2006

Keywords

  • Extended shuttle
  • Import of folded and oligomeric protein
  • Peroxisomal RADAR
  • Peroxisomal matrix protein import
  • Quality-control
  • Shuttling receptor

ASJC Scopus subject areas

  • Molecular Biology
  • Cell Biology

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