Molecular Biology of the Cell
Geisel School of Medicine
Secretory proteins are exported from the endoplasmic reticulum (ER) in transport vesicles formed by the coat protein complex II (COPII). We detected Erv26p as an integral membrane protein that was efficiently packaged into COPII vesicles and cycled between the ER and Golgi compartments. The erv26Δ mutant displayed a selective secretory defect in which the pro-form of vacuolar alkaline phosphatase (pro-ALP) accumulated in the ER, whereas other secretory proteins were transported at wild-type rates. In vitro budding experiments demonstrated that Erv26p was directly required for packaging of pro-ALP into COPII vesicles. Moreover, Erv26p was detected in a specific complex with pro-ALP when immunoprecipitated from detergent-solublized ER membranes. Based on these observations, we propose that Erv26p serves as a transmembrane adaptor to link specific secretory cargo to the COPII coat. Because ALP is a type II integral membrane protein in yeast, these findings imply that an additional class of secretory cargo relies on adaptor proteins for efficient export from the ER.
Bue CA, Bentivoglio CM, Barlowe C. Erv26p directs pro-alkaline phosphatase into endoplasmic reticulum-derived coat protein complex II transport vesicles. Mol Biol Cell. 2006 Nov;17(11):4780-9. doi: 10.1091/mbc.e06-05-0455. Epub 2006 Sep 6. PMID: 16957051; PMCID: PMC1635384.
Dartmouth Digital Commons Citation
Bue, Catherine A.; Bentivoglio, Christine M.; and Barlowe, Charles, "Erv26p Directs Pro-Alkaline Phosphatase into Endoplasmic Reticulum–derived Coat Protein Complex II Transport Vesicles" (2006). Dartmouth Scholarship. 3774.