Quantitative proteomics analysis of the secretory pathway

Cell. 2006 Dec 15;127(6):1265-81. doi: 10.1016/j.cell.2006.10.036.


We report more than 1400 proteins of the secretory-pathway proteome and provide spatial information on the relative presence of each protein in the rough and smooth ER Golgi cisternae and Golgi-derived COPI vesicles. The data support a role for COPI vesicles in recycling and cisternal maturation, showing that Golgi-resident proteins are present at a higher concentration than secretory cargo. Of the 1400 proteins, 345 were identified as previously uncharacterized. Of these, 230 had their subcellular location deduced by proteomics. This study provides a comprehensive catalog of the ER and Golgi proteomes with insight into their identity and function.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Coat Protein Complex I
  • Endoplasmic Reticulum / chemistry*
  • Golgi Apparatus / chemistry*
  • Liver / chemistry
  • Liver / cytology
  • Protein Transport
  • Proteins / analysis*
  • Proteins / isolation & purification*
  • Proteomics*
  • Rats
  • SNARE Proteins / isolation & purification
  • Tandem Mass Spectrometry
  • rab GTP-Binding Proteins / genetics
  • rab GTP-Binding Proteins / isolation & purification


  • Coat Protein Complex I
  • Proteins
  • SNARE Proteins
  • rab GTP-Binding Proteins