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Quantitative Proteomics Analysis of the Secretory Pathway

2006; Cell Press; Volume: 127; Issue: 6 Linguagem: Inglês

10.1016/j.cell.2006.10.036

1097-4172

Annalyn Gilchrist, Catherine Au, Johan Hiding, Alexander W. Bell, Julia Fernández-Rodrı́guez, Souad Lesimple, Hisao Nagaya, Line Roy, Sara J.C. Gosline, Michael Hallett, Jacques Paiement, Robert E. Kearney, Tommy Nilsson, John Bergeron,

Nuclear Structure and Function

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.