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J. Biol. Chem., Vol. 277, Issue 25, 22395-22401, June 21, 2002
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,
From the Department of Molecular and Cell Biology, Howard Hughes
Medical Institute, University of California,
Berkeley, California 94720
The yeast plasma membrane
H+-ATPase Pma1p is one of the most abundant proteins
to traverse the secretory pathway. Newly synthesized Pma1p exits the
endoplasmic reticulum (ER) via COPII-coated vesicles bound for the
Golgi. Unlike most secreted proteins, efficient incorporation of Pma1p
into COPII vesicles requires the Sec24p homolog Lst1p, suggesting a
unique role for Lst1p in ER export. Vesicles formed with mixed
Sec24p-Lst1p coats are larger than those with Sec24p alone. Here, we
examined the relationship between Pma1p biosynthesis and the
requirement for this novel coat subunit. We show that Pma1p forms a
large oligomeric complex of >1 MDa in the ER, which is packaged into
COPII vesicles. Furthermore, oligomerization of Pma1p is linked to
membrane lipid composition; Pma1p is rendered monomeric in cells
depleted of ceramide, suggesting that association with lipid rafts may
influence oligomerization. Surprisingly, monomeric Pma1p present in
ceramide-deficient membranes can be exported from the ER in COPII
vesicles in a reaction that is stimulated by Lst1p. We suggest that
Lst1p directly conveys Pma1p into a COPII vesicle and that the larger
size of mixed Sec24pLst1p COPII vesicles is not essential to the
packaging of large oligomeric complexes.
Supported by a fellowship from the Human Frontiers Science Program.
§
To whom correspondence should be addressed. Tel.: 510-642-5686;
Fax: 510-642-7846; E-mail: schekman@uclink4.berkeley.edu.
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