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BI-DIRECTIONAL PROTEIN TRANSPORT BETWEEN THE ER AND GOLGI
Abstract
▪ Abstract The endoplasmic reticulum (ER) and the Golgi comprise the first two steps in protein secretion. Vesicular carriers mediate a continuous flux of proteins and lipids between these compartments, reflecting the transport of newly synthesized proteins out of the ER and the retrieval of escaped ER residents and vesicle machinery. Anterograde and retrograde transport is mediated by distinct sets of cytosolic coat proteins, the COPII and COPI coats, respectively, which act on the membrane to capture cargo proteins into nascent vesicles. We review the mechanisms that govern coat recruitment to the membrane, cargo capture into a transport vesicle, and accurate delivery to the target organelle.
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Proteins are shuttled from the ER to the Golgi apparatus by COPII vesicles coated with the cytosolic Sec23/Sec24 adaptors heterodimers that play a key role in cargo recruitment to the transport vesicle.
“Proteins are shuttled from the ER to the Golgi apparatus by COPII vesicles coated with the cytosolic Sec23/Sec24 adaptors heterodimers that play a key role in cargo recruitment to the transport vesicle (54).”
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Metadata
- Authors
- Lee, M. C. S., Miller, E. A., Goldberg, J., Orci, L., & Schekman, R.
- Affiliations
- Howard Hughes Medical Institute and Department of Molecular and Cell Biology, University of California, Berkeley, California;
- Howard Hughes Medical Institute and Memorial Sloan-Kettering Cancer Center, New York;
- Department of Morphology, University of Geneva Medical School, Switzerland;
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2004-11-01
- Volume
- 20
- Issue
- 1
- Pages
- 87-123
- ISSN
- 1081-0706
- 1530-8995
- Cited by
- 813
- References
- 1
- Language
- en
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