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Published 23 December 2002. doi:10.1083/jcb.200208074
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© The Rockefeller University Press, 0021-9525/2002/12/915 $5.00
The Journal of Cell Biology, Volume 159, Number 6, 915-921

Report

Concentrative sorting of secretory cargo proteins into COPII-coated vesicles



Per Malkus, Feng Jiang and Randy Schekman

Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720

Address correspondence to Randy Schekman, Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, Berkeley, Berkeley, CA 94720. Tel.: (510) 642-5686. Fax: (510) 642-7846. E-mail: schekman{at}uclink4.berkeley.edu

Here, we show that efficient transport of membrane and secretory proteins from the ER of Saccharomyces cerevisiae requires concentrative and signal-mediated sorting. Three independent markers of bulk flow transport out of the ER indicate that in the absence of an ER export signal, molecules are inefficiently captured into coat protein complex II (COPII)-coated vesicles. A soluble secretory protein, glycosylated pro–{alpha}-factor (gp{alpha}f), was enriched ~20 fold in these vesicles relative to bulk flow markers. In the absence of Erv29p, a membrane protein that facilitates gp{alpha}f transport (Belden and Barlowe, 2001), gp{alpha}f is packaged into COPII vesicles as inefficiently as soluble bulk flow markers. We also found that a plasma membrane protein, the general amino acid permease (Gap1p), is enriched approximately threefold in COPII vesicles relative to membrane phospholipids. Mutation of a diacidic sequence present in the COOH-terminal cytosolic domain of Gap1p eliminated concentrative sorting of this protein.

Key Words: intracellular membranes; endoplasmic reticulum; COPII-coated vesicle; protein transport; protein sorting signals


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