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

Quantitative proteomics analysis of the secretory pathway

Annalyn Gilchrist  1 , Catherine E Au, Johan Hiding, Alexander W Bell, Julia Fernandez-Rodriguez, Souad Lesimple, Hisao Nagaya, Line Roy, Sara J C Gosline, Michael Hallett, Jacques Paiement, Robert E Kearney, Tommy Nilsson, John J M Bergeron
Affiliations
Free article

Quantitative proteomics analysis of the secretory pathway

Annalyn Gilchrist et al. Cell. .
Free article

Abstract

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.

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