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Role of Erv29p in Collecting Soluble Secretory Proteins into ER-Derived Transport Vesicles

Belden, William J., Barlowe, Charles·2001·Science

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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Metadata

Authors
Belden, W. J., & Barlowe, C.
Venue
Science
Published
2001-11-16
Volume
294
Issue
5546
Pages
1528-1531
ISSN
  • 0036-8075 (ISSN-L)
  • 1095-9203
OpenAlex
W2041674095
Cited by
214
References
0
FWCI
5.06
Type
journal article
Language
en
Open access
closed

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CoChat. (2026). Citation check: Role of Erv29p in Collecting Soluble Secretory Proteins into ER-Derived Transport Vesicles. https://app.cochat.ai/papers/10.1126/science.1065224
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Belden, W. J., & Barlowe, C. (2001). Role of Erv29p in Collecting Soluble Secretory Proteins into ER-Derived Transport Vesicles. Science. https://doi.org/10.1126/science.1065224

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.