Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles

W. J. Belden; C. Barlowe

doi:10.1126/science.1065224

Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles

W. J. Belden, C. Barlowe

Research output: Contribution to journal › Article › peer-review

178 Scopus citations

Abstract

Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by "bulk flow" or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-α-factor (gpαf) Into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gpαf complex was isolated from ER-derived transport vesicles. In vivo, export of gpαf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.

Original language	English (US)
Pages (from-to)	1528-1531
Number of pages	4
Journal	Science
Volume	294
Issue number	5546
DOIs	https://doi.org/10.1126/science.1065224
State	Published - Nov 16 2001
Externally published	Yes

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title = "Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles",

abstract = "Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by {"}bulk flow{"} or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-α-factor (gpαf) Into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gpαf complex was isolated from ER-derived transport vesicles. In vivo, export of gpαf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.",

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T1 - Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles

AU - Belden, W. J.

AU - Barlowe, C.

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N2 - Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by "bulk flow" or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-α-factor (gpαf) Into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gpαf complex was isolated from ER-derived transport vesicles. In vivo, export of gpαf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.

AB - Proteins are transported from the endoplasmic reticulum (ER) in vesicles formed by coat protein complex II (COPII). Soluble secretory proteins are thought to leave the ER in these vesicles by "bulk flow" or through recognition by hypothetical shuttling receptors. We found that Erv29p, a conserved transmembrane protein, was directly required for packaging glycosylated pro-α-factor (gpαf) Into COPII vesicles in Saccharomyces cerevisiae. Further, an Erv29p-gpαf complex was isolated from ER-derived transport vesicles. In vivo, export of gpαf from the ER was saturable and depended on the expression level of Erv29p. These results indicate that membrane receptors can link soluble cargo proteins to the COPII coat.

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Role of Erv29p in collecting soluble secretory proteins into ER-derived transport vesicles

Abstract

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