Import of proteins into peroxisomes: piggybacking to a new home away from home

Open Biol. 2015 Nov;5(11):150148. doi: 10.1098/rsob.150148.

Abstract

Peroxisomes are capable of importing folded and oligomeric proteins. However, it is a matter of dispute whether oligomer import by peroxisomes is the exception or the rule. Here, I argue for a clear distinction between homo-oligomeric proteins that are essentially peroxisomal, and dually localized hetero-oligomers that access the peroxisome by piggyback import, localizing there in limited number, whereas the majority remain in the cytosol. Homo-oligomeric proteins comprise the majority of all peroxisomal matrix proteins. There is evidence that binding by Pex5 in the cytosol can regulate their oligomerization state before import. The hetero-oligomer group is made up of superoxide dismutase and lactate dehydrogenase. These proteins have evolved mechanisms that render import inefficient and retain the majority of proteins in the cytosol.

Keywords: PTS1; Pex5; cellular organelles; peroxisome; piggyback import; protein import.

Publication types

  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Humans
  • Molecular Sequence Data
  • Peroxisome-Targeting Signal 1 Receptor
  • Peroxisomes / metabolism*
  • Protein Multimerization
  • Protein Transport
  • Receptors, Cytoplasmic and Nuclear / chemistry
  • Receptors, Cytoplasmic and Nuclear / metabolism*

Substances

  • PEX5 protein, human
  • Peroxisome-Targeting Signal 1 Receptor
  • Receptors, Cytoplasmic and Nuclear