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PMID: 22193160 Published · epublish English Journal Article Research Support, Non-U.S. Gov't Review

COPII and the regulation of protein sorting in mammals.

Nature cell biology ·Vol. 14 ·No. 1 ·2011-12-22 ·Pages 20-8

Zanetti G, Pahuja KB, Studer S, Shim S, Schekman R

Abstract

Secretory proteins are transported to the Golgi complex in vesicles that bud from the endoplasmic reticulum. The cytoplasmic coat protein complex II (COPII) is responsible for cargo sorting and vesicle morphogenesis. COPII was first described in Saccharomyces cerevisiae, but its basic function is conserved throughout all eukaryotes. Nevertheless, the COPII coat has adapted to the higher complexity of mammalian physiology, achieving more sophisticated levels of secretory regulation. In this review we cover aspects of mammalian COPII-mediated regulation of secretion, in particular related to the function of COPII paralogues, the spatial organization of cargo export and the role of accessory proteins.

MeSH Terms
Animals COP-Coated Vesicles/metabolism Endoplasmic Reticulum/metabolism Golgi Apparatus/metabolism Humans Mammals Protein Transport Secretory Pathway/physiology
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Zanetti Giulia
Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, California 94720, USA.
Pahuja Kanika Bajaj
Studer Sean
Shim Soomin
Schekman Randy
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Article Info
Journal
Nature cell biology
Abbr.
Nat Cell Biol
ISSN
1476-4679
Published
2011-12-22
Epub
2011-00-22
Pages
20-8
Language
English
Region
England
NLM ID
100890575
Subset
IM
Grants
Howard Hughes Medical Institute · United States
Corrections
ErratumIn
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