The intrinsically disordered nature of the peroxisomal protein translocation machinery

FEBS J. 2019 Jan;286(1):24-38. doi: 10.1111/febs.14704. Epub 2018 Dec 1.

Abstract

Despite having a membrane that is impermeable to all but the smallest of metabolites, peroxisomes acquire their newly synthesized (cytosolic) matrix proteins in an already folded conformation. In some cases, even oligomeric proteins have been reported to translocate the organelle membrane. The protein sorting machinery that accomplishes this feat must be rather flexible and, unsurprisingly, several of its key components have large intrinsically disordered domains. Here, we provide an overview on these domains and their interactions trying to infer their functional roles in this protein sorting pathway.

Keywords: docking/translocation module; intrinsic disorder; matrix protein import; peroxins; peroxisomes.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Humans
  • Intrinsically Disordered Proteins / metabolism*
  • Peroxisomes / metabolism*
  • Protein Domains
  • Protein Interaction Domains and Motifs*
  • Protein Transport
  • Signal Transduction

Substances

  • Intrinsically Disordered Proteins