[HTML][HTML] Quantitative proteomics analysis of the secretory pathway
A Gilchrist, CE Au, J Hiding, AW Bell… - Cell, 2006 - cell.com
A Gilchrist, CE Au, J Hiding, AW Bell, J Fernandez-Rodriguez, S Lesimple, H Nagaya, L Roy…
Cell, 2006•cell.comWe 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 …
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 …
Summary
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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