Protein Folding and Quality Control in the ER

被引：252

作者：

Araki, Kazutaka ^{[1
]}

Nagata, Kazuhiro ^{[1
]}

机构：

[1] Kyoto Sangyo Univ, Lab Mol & Cellular Biol, Fac Life Sci, Kita Ku, Kyoto 8038555, Japan

来源：

COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY | 2011年 / 3卷 / 11期

关键词：

RETICULUM-ASSOCIATED-DEGRADATION; MHC CLASS-I; DISULFIDE-ISOMERASE FAMILY; UBIQUITIN LIGASE COMPLEX; SIGNAL PEPTIDE PEPTIDASE; TAIL-ANCHORED PROTEIN; ENDOPLASMIC-RETICULUM; MISFOLDED GLYCOPROTEINS; MEMBRANE-PROTEIN; MOLECULAR CHAPERONE;

D O I：

10.1101/cshperspect.a007526

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

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.

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页数：25

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