title: Roles of molecular chaperones in endoplasmic reticulum (ER) quality control and ER-associated degradation (ERAD).
abstract: Secreted proteins are synthesized at the endoplasmic reticulum (ER), and a quality control mechanism in the ER is essential to maintain secretory pathway homeostasis. Newly synthesized soluble and integral membrane secreted proteins fold into their native conformations with the aid of ER molecular chaperones before they are transported to post-ER compartments. However, terminally mis-folded proteins may be retained in the ER and degraded by a process called ER-associated degradation (ERAD). Recent studies using yeast have shown that molecular chaperones both in the ER and in the cytosol play key roles during the ERAD of mis-folded proteins. One important role for chaperones during ERAD is to prevent substrate protein aggregation. Substrate selection is another important role for molecular chaperones during ERAD.
authors.affiliation: Department of Chemistry, Graduate School of Science, Nagoya University, Nagoya 464-8602. shuh@biochem.chem.nagoya-u.ac.jp
authors.forename: Shuh-ichi
authors.initials: S
authors.lastname: Nishikawa
authors.forename: Jeffrey L
authors.initials: JL
authors.lastname: Brodsky
authors.forename: Kunio
authors.initials: K
authors.lastname: Nakatsukasa
mesh_terms: D003600:Cytosol / Q000502:physiology; D004721:Endoplasmic Reticulum / Q000502:physiology*; D018840:HSP70 Heat-Shock Proteins / Q000502:physiology*; D008361:Mannosidases / Q000378:metabolism; D008954:Models, Biological; D018832:Molecular Chaperones / Q000502:physiology*; D017510:Protein Folding; D011499:Protein Processing, Post-Translational / Q000502:physiology
chemical_list: D018840:HSP70 Heat-Shock Proteins; D018832:Molecular Chaperones; D008361:Mannosidases; C046090:mannosyl-oligosaccharide 1,2-alpha-mannosidase