Localization of Rab proteins to peroxisomes: a proteomics and immunofluorescence study

FEBS Lett. 2013 Feb 14;587(4):328-38. doi: 10.1016/j.febslet.2012.12.025. Epub 2013 Jan 16.

Abstract

A proteomics screen was initiated to identify Rab proteins regulating transport to and away from peroxisomes. Mass spectrometry-based protein correlation profiling of rat liver organelles and immunofluorescence analysis of the peroxisome candidate Rab proteins revealed Rab6, Rab10, Rab14 and Rab18 to associate with the peroxisomal membrane. While Rab14 localized to peroxisomes predominantly in its dominant-active form, other Rab proteins associated with peroxisomes in both their GTP- and GDP-bound state. In summary, our data suggest that Rab6, Rab10, Rab14 and Rab18 associate with the peroxisomal compartment and similar as previously shown for Rab8, Rab18 in its GDP-bound state favors peroxisome proliferation.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Cell Line
  • Guanosine Diphosphate / metabolism
  • Hepatocytes / cytology
  • Hepatocytes / enzymology*
  • Hepatocytes / metabolism
  • Humans
  • Luminescent Proteins / genetics
  • Luminescent Proteins / metabolism
  • Mice
  • Microscopy, Fluorescence
  • Mutant Proteins / genetics
  • Mutant Proteins / metabolism
  • Peroxisomes / enzymology*
  • Peroxisomes / metabolism
  • Protein Transport
  • Proteomics / methods
  • Rats
  • Recombinant Fusion Proteins / metabolism
  • Up-Regulation
  • rab GTP-Binding Proteins / biosynthesis
  • rab GTP-Binding Proteins / genetics
  • rab GTP-Binding Proteins / metabolism*

Substances

  • Luminescent Proteins
  • Mutant Proteins
  • Rab18 protein, mouse
  • Rab6 protein
  • Recombinant Fusion Proteins
  • Guanosine Diphosphate
  • Rab10 protein, human
  • Rab14 protein, human
  • Rab18 protein, rat
  • rab GTP-Binding Proteins