title: COPII and the regulation of protein sorting in mammals.
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.
authors.affiliation: Department of Molecular and Cell Biology and Howard Hughes Medical Institute, University of California at Berkeley, Berkeley, California 94720, USA.
authors.forename: Giulia
authors.initials: G
authors.lastname: Zanetti
authors.forename: Kanika Bajaj
authors.initials: KB
authors.lastname: Pahuja
authors.forename: Sean
authors.initials: S
authors.lastname: Studer
authors.forename: Soomin
authors.initials: S
authors.lastname: Shim
authors.forename: Randy
authors.initials: R
authors.lastname: Schekman
mesh_terms: D000818:Animals; D022181:COP-Coated Vesicles / Q000378:metabolism*; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006056:Golgi Apparatus / Q000378:metabolism*; D006801:Humans; D008322:Mammals; D021381:Protein Transport; D055571:Secretory Pathway / Q000502:physiology*