title: Versatility of the endoplasmic reticulum protein folding factory.
abstract: The endoplasmic reticulum (ER) is dedicated to import, folding and assembly of all proteins that travel along or reside in the secretory pathway of eukaryotic cells. Folding in the ER is special. For instance, newly synthesized proteins are N-glycosylated and by default form disulfide bonds in the ER, but not elsewhere in the cell. In this review, we discuss which features distinguish the ER as an efficient folding factory, how the ER monitors its output and how it disposes of folding failures.
authors.affiliation: Department of Cellular Protein Chemistry, Bijvoet Center, Utrecht University, The Netherlands.
authors.forename: Eelco
authors.initials: E
authors.lastname: van Anken
authors.forename: Ineke
authors.initials: I
authors.lastname: Braakman
mesh_terms: D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006023:Glycoproteins / Q000378:metabolism; D006031:Glycosylation; D057927:Hydrophobic and Hydrophilic Interactions; D008954:Models, Biological; D018832:Molecular Chaperones / Q000096:biosynthesis / Q000737:chemistry / Q000378:metabolism; D011489:Protein Denaturation; D017510:Protein Folding; D011786:Quality Control; D015398:Signal Transduction / Q000502:physiology; D025801:Ubiquitin / Q000378:metabolism
chemical_list: D006023:Glycoproteins; D018832:Molecular Chaperones; D025801:Ubiquitin