PEX19 is a predominantly cytosolic chaperone and import receptor for class 1 peroxisomal membrane proteins

Jacob M. Jones, James C. Morrell, Stephen J. Gould

Research output: Contribution to journalArticlepeer-review

Abstract

Integral peroxisomal membrane proteins (PMPs) are synthesized in the cytoplasm and imported posttranslationally. Here, we demonstrate that PEX19 binds and stabilizes newly synthesized PMPs in the cytosol, binds to multiple PMP targeting signals (mPTSs), interacts with the hydrophobic domains of PMP targeting signals, and is essential for PMP targeting and import. These results show that PEX19 functions as both a chaperone and an import receptor for newly synthesized PMPs. We also demonstrate the existence of two PMP import mechanisms and two classes of mPTSs: class 1 mPTSs, which are bound by PEX19 and imported in a PEX19-dependent manner, and class 2 mPTSs, which are not bound by PEX19 and mediate protein import independently of PEX19.

Original languageEnglish (US)
Pages (from-to)57-67
Number of pages11
JournalJournal of Cell Biology
Volume164
Issue number1
DOIs
StatePublished - Jan 2004

Keywords

  • PEX3
  • Peroxisome
  • Posttranslational
  • Protein import
  • Zellweger syndrome

ASJC Scopus subject areas

  • Cell Biology

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