title: Protein folding and quality control in the ER.
abstract: The endoplasmic reticulum (ER) uses an elaborate surveillance system called the ER quality control (ERQC) system. The ERQC facilitates folding and modification of secretory and membrane proteins and eliminates terminally misfolded polypeptides through ER-associated degradation (ERAD) or autophagic degradation. This mechanism of ER protein surveillance is closely linked to redox and calcium homeostasis in the ER, whose balance is presumed to be regulated by a specific cellular compartment. The potential to modulate proteostasis and metabolism with chemical compounds or targeted siRNAs may offer an ideal option for the treatment of disease.
authors.affiliation: Laboratory of Molecular and Cellular Biology, Faculty of Life Sciences, Kyoto Sangyo University, Kamigamo, Kita-ku, Kyoto 803-8555, Japan.
authors.forename: Kazutaka
authors.initials: K
authors.lastname: Araki
authors.forename: Kazuhiro
authors.initials: K
authors.lastname: Nagata
mesh_terms: D002118:Calcium / Q000378:metabolism; D020013:Calcium Signaling; D004721:Endoplasmic Reticulum / Q000378:metabolism*; D006706:Homeostasis; D008954:Models, Biological; D018832:Molecular Chaperones / Q000737:chemistry / Q000378:metabolism; D010084:Oxidation-Reduction; D014176:Protein Biosynthesis; D017510:Protein Folding; D021381:Protein Transport
chemical_list: D018832:Molecular Chaperones; D002118:Calcium