Quantitative Proteomics Analysis of the Secretory Pathway

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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. © 2006 Elsevier Inc. All rights reserved.

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Gilchrist, A., Au, C. E., Hiding, J., Bell, A. W., Fernandez-Rodriguez, J., Lesimple, S., … Bergeron, J. J. M. (2006). Quantitative Proteomics Analysis of the Secretory Pathway. Cell, 127(6), 1265–1281. https://doi.org/10.1016/j.cell.2006.10.036

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