Import of peroxisomal membrane proteins: the interplay of Pex3p- and Pex19p-mediated interactions

Biochim Biophys Acta. 2006 Dec;1763(12):1639-46. doi: 10.1016/j.bbamcr.2006.09.030. Epub 2006 Sep 26.


In contrast to the molecular mechanisms underlying import of peroxisomal matrix proteins, those involving the transport of membrane proteins remain rather elusive. At present, two targeting routes for peroxisomal membrane proteins (PMPs) have been depicted: class I PMPs are targeted from the cytoplasm directly to the peroxisome membrane, and class II PMPs are sorted indirectly to peroxisomes via the endoplasmic reticulum (ER). In addition, three peroxins--Pex3p, Pex16p, and Pex19p - have been identified as essential factors for PMP assembly in several species including humans: Pex19p is a predominantly cytoplasmic protein that shows a broad PMP-binding specificity; Pex3p serves as the membrane-anchoring site for Pex19p; and Pex16p - a protein absent in most yeasts--is thought to provide the initial scaffold for recruiting the protein import machinery required for peroxisome membrane biogenesis. Remarkably, the function of Pex16p does not appear to be conserved between different species. In addition, significant disagreement exists about whether Pex19p has a chaperone-like role in the cytosol or at the peroxisome membrane and/or functions as a cycling import receptor for newly synthesized PMPs. Here we review the recent progress made in our understanding of the role of two key players in PMP biogenesis, Pex3p and Pex19p.

Publication types

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

MeSH terms

  • Endoplasmic Reticulum / metabolism
  • Humans
  • Lipoproteins / metabolism
  • Membrane Proteins / metabolism*
  • Peroxins
  • Peroxisomes / metabolism*
  • Protein Binding
  • Protein Transport
  • Saccharomyces cerevisiae Proteins / metabolism


  • Lipoproteins
  • Membrane Proteins
  • PEX3 protein, S cerevisiae
  • Peroxins
  • Pex3 protein, human
  • Saccharomyces cerevisiae Proteins
  • PEX19 protein, human