title: The action of molecular chaperones in the early secretory pathway.
abstract: The endoplasmic reticulum (ER) serves as a way-station during the biogenesis of nearly all secreted proteins, and associated with or housed within the ER are factors required to catalyze their import into the ER and facilitate their folding. To ensure that only properly folded proteins are secreted and to temper the effects of cellular stress, the ER can target aberrant proteins for degradation and/or adapt to the accumulation of misfolded proteins. Molecular chaperones play critical roles in each of these phenomena.
authors.affiliation: Department of Biological Sciences, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, USA.
authors.forename: S W
authors.initials: SW
authors.lastname: Fewell
authors.forename: K J
authors.initials: KJ
authors.lastname: Travers
authors.forename: J S
authors.initials: JS
authors.lastname: Weissman
authors.forename: J L
authors.initials: JL
authors.lastname: Brodsky
mesh_terms: D000818:Animals; D001692:Biological Transport; D004721:Endoplasmic Reticulum / Q000378:metabolism; D006801:Humans; D008565:Membrane Proteins / Q000378:metabolism; D018832:Molecular Chaperones / Q000276:immunology / Q000378:metabolism*; D017510:Protein Folding; D011506:Proteins / Q000378:metabolism*; D011786:Quality Control
chemical_list: D008565:Membrane Proteins; D018832:Molecular Chaperones; D011506:Proteins