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A more recent version of this article appeared on March 1, 2002
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Submitted on October 12, 2001
Revised on November 20, 2001
Accepted on November 29, 2001
1 Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755
* Corresponding author. E-mail address: barlowe{at}dartmouth.edu.
Erv14p is a conserved integral membrane protein that traffics in COPII coated vesicles and localizes to the early secretory pathway in yeast. Deletion of ERV14 causes a defect in polarized growth because Axl2p, a transmembrane secretory protein, accumulates in the ER and is not delivered to its site of function on the cell surface. Here we show that Erv14p is required for selection of Axl2p into COPII vesicles and for efficient formation of these vesicles. Erv14p binds to subunits of the COPII coat and binding depends on conserved residues in a cytoplasmically exposed loop domain of Erv14p. When mutations are introduced into this loop, an Erv14p-Axl2p complex accumulates in the ER, suggesting that Erv14p links Axl2p to the COPII coat. Based on these results and further genetic experiments, we propose Erv14p coordinates COPII vesicle formation with incorporation of specific secretory cargo.
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