Quantitative proteomics analysis of the secretory pathway.
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.
Gilchrist
Annalyn
A
Department of Anatomy and Cell Biology, McGill University, 3640 University Street, Montreal, Quebec H3A 2B2, Canada.
Au
Catherine E
CE
Hiding
Johan
J
Bell
Alexander W
AW
Fernandez-Rodriguez
Julia
J
Lesimple
Souad
S
Nagaya
Hisao
H
Roy
Line
L
Gosline
Sara J C
SJ
Hallett
Michael
M
Paiement
Jacques
J
Kearney
Robert E
RE
Nilsson
Tommy
T
Bergeron
John J M
JJ
D000818:Animals; D020755:Coat Protein Complex I; D004721:Endoplasmic Reticulum / Q000737:chemistry*; D006056:Golgi Apparatus / Q000737:chemistry*; D008099:Liver / Q000737:chemistry / Q000166:cytology; D021381:Protein Transport; D011506:Proteins / Q000032:analysis* / Q000302:isolation & purification*; D040901:Proteomics; D051381:Rats; D050600:SNARE Proteins / Q000302:isolation & purification; D053719:Tandem Mass Spectrometry; D020691:rab GTP-Binding Proteins / Q000235:genetics / Q000302:isolation & purification
D020755:Coat Protein Complex I; D011506:Proteins; D050600:SNARE Proteins; D020691:rab GTP-Binding Proteins