Letter abstract
Nature Cell Biology 6, 1189 - 1194 (2004)
Published online: 31 October 2004 | doi:10.1038/ncb1195
Sorting signals can direct receptor-mediated export of soluble proteins into COPII vesicles
Stefan Otte1,2 & Charles Barlowe1
Soluble secretory proteins are first translocated across endoplasmic reticulum (ER) membranes and folded in a specialized ER luminal environment. Fully folded and assembled secretory cargo are then segregated from ER-resident proteins into COPII-derived vesicles or tubular elements for anterograde transport. Mechanisms of bulk-flow, ER-retention and receptor-mediated export have been suggested to operate during this transport step, although these mechanisms are poorly understood1, 2, 3, 4, 5, 6, 7. In yeast, there is evidence to suggest that Erv29p functions as a transmembrane receptor for the export of certain soluble cargo proteins including glycopro-
-factor (gpf), the precursor of -factor mating pheromone8. Here we identify a hydrophobic signal within the pro-region of gpf that is necessary for efficient packaging into COPII vesicles and for binding to Erv29p. When fused to Kar2p, an ER-resident protein, the pro-region sorting signal was sufficient to direct Erv29p-dependent export of the fusion protein into COPII vesicles. These findings indicate that specific motifs within soluble secretory proteins function in receptor-mediated export from the ER. Moreover, positive sorting signals seem to predominate over potential ER-retention mechanisms that may operate in localizing ER-resident proteins such as Kar2p.
- Department of Biochemistry, Dartmouth Medical School, Hanover, NH 03755, USA.
- Present address: Department of Biochemistry and Molecular Genetics, University of Illinois at Chicago, Chicago, IL 60607, USA.
Correspondence to: Charles Barlowe1 e-mail: barlowe@dartmouth.edu
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