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Vol. 13, Issue 3, 880-891, March 2002
Department of Biochemistry, Dartmouth Medical School, Hanover, New
Hampshire 03755
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 endoplasmic reticulum and is not delivered to its site of
function on the cell surface. Herein, 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 endoplasmic reticulum,
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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