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(Received for publication, May 15, 1996, and in revised form, July 31, 1996)
From the Department of Biochemistry, Dartmouth Medical School,
Hanover, New Hampshire 03755
COPII-coated endoplasmic reticulum (ER)-derived
transport vesicles contain a distinct set of membrane-bound
polypeptides. We have obtained the NH2-terminal amino acid
sequence of polypeptide constituents found on purified vesicles and in
this report investigate the 24- and 25-kDa species. The 24-kDa protein
is identical to Emp24p, a type I transmembrane protein that is required
for transport of a subset of secretory proteins from the ER to the
Golgi complex (Schimmöller, F., Singer-Krüger, B.,
Schröder, S., Krüger, U., Barlowe, C., and Riezman, H. (1995) EMBO J. 14, 1329-1339). The 25-kDa protein, termed
Erv25p (
Volume 271, Number 43,
Issue of October 25, 1996
pp. 26939-26946
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.
esicle protein of 25 kDa),
corresponds to an open reading frame found on chromosome XIII of
Saccharomyces cerevisiae. Erv25p shares overall sequence
identity with Emp24p, but the two proteins are not functionally
interchangeable. Antibodies directed against Erv25p reveal that Emp24p
and Erv25p depend on each other for stability and form a protein
complex that can be isolated after chemical cross-linking. Yeast
strains lacking Erv25p (erv25
) are viable and display
the same selective defect in transport of secretory proteins from the
ER to Golgi complex as an emp24 strain. A cell-free
assay that measures vesicle formation from ER membranes demonstrates
that Erv25p and Emp24p are incorporated equally into ER-derived
vesicles when COPII-coated budding is reconstituted. Vesicle formation
from an erv25 strain, an emp24 strain and
a double erv25 emp24 strain proceed at wild-type
levels; however, incorporation of the Erv25p or the Emp24p protein into
COPII-coated vesicles requires expression of both subunits. A potential
model for transport of the Erv25p-Emp24p complex between the ER and
Golgi compartments is discussed.
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S. Springer, E. Chen, R. Duden, M. Marzioch, A. Rowley, S. Hamamoto, S. Merchant, and R. Schekman From the Cover: The p24 proteins are not essential for vesicular transport in Saccharomyces cerevisiae PNAS, April 11, 2000; 97(8): 4034 - 4039. [Abstract] [Full Text] [PDF]
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