PMID:12499351

Citation	Malkus, P, Jiang, F and Schekman, R (2002) Concentrative sorting of secretory cargo proteins into COPII-coated vesicles. J. Cell Biol. 159:915-21
Abstract	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 (gpalphaf), was enriched approximately 20 fold in these vesicles relative to bulk flow markers. In the absence of Erv29p, a membrane protein that facilitates gpalphaf transport (Belden and Barlowe, 2001), gpalphaf 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.
Links	PubMed PMC2173974 Online version:10.1083/jcb.200208074
Keywords	Amino Acid Sequence; Amino Acid Transport Systems; COP-Coated Vesicles/metabolism; Cell Membrane/metabolism; Cytosol/metabolism; Databases as Topic; Endoplasmic Reticulum/metabolism; Immunoblotting; Microsomes/metabolism; Molecular Sequence Data; Mutation; Plasmids/metabolism; Protein Precursors/metabolism; Protein Sorting Signals; Protein Structure, Tertiary; Protein Transport; Saccharomyces cerevisiae/metabolism; Saccharomyces cerevisiae Proteins/metabolism; Sequence Homology, Amino Acid; Signal Transduction; ras GTPase-Activating Proteins/metabolism
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