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.
引用
收藏
页数:25
相关论文
共 245 条
[1]   N-glycan structures: recognition and processing in the ER [J].
Aebi, Markus ;
Bernasconi, Riccardo ;
Clerc, Simone ;
Molinari, Maurizio .
TRENDS IN BIOCHEMICAL SCIENCES, 2010, 35 (02) :74-82
[2]   Protein quality control in the early secretory pathway [J].
Anelli, Tiziana ;
Sitia, Roberto .
EMBO JOURNAL, 2008, 27 (02) :315-327
[3]   Glutathione- and non-glutathione-based oxidant control in the endoplasmic reticulum [J].
Appenzeller-Herzog, Christian .
JOURNAL OF CELL SCIENCE, 2011, 124 (06) :847-855
[4]   Disulphide production by Ero1α-PDI relay is rapid and effectively regulated [J].
Appenzeller-Herzog, Christian ;
Riemer, Jan ;
Zito, Ester ;
Chin, King-Tung ;
Ron, David ;
Spiess, Martin ;
Ellgaard, Lars .
EMBO JOURNAL, 2010, 29 (19) :3318-3329
[5]   The human PDI family: Versatility packed into a single fold [J].
Apperizeller-Herzog, Christian ;
Ellgaard, Lars .
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2008, 1783 (04) :535-548
[6]   Endoplasmic reticulum (ER) mannosidase I is compartmentalized and required for N-glycan trimming to Man5-6GlcNAc2 in glycoprotein ER-associated degradation [J].
Avezov, Edward ;
Frenkel, Zehavit ;
Ehrlich, Marcelo ;
Herscovics, Annette ;
Lederkremer, Gerardo Z. .
MOLECULAR BIOLOGY OF THE CELL, 2008, 19 (01) :216-225
[7]   Protein dislocation from the ER [J].
Bagola, Katrin ;
Mehnert, Martin ;
Jarosch, Ernst ;
Sommer, Thomas .
BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES, 2011, 1808 (03) :925-936
[8]   Identification of SVIP as an endogenous inhibitor of endoplasmic reticulum-associated degradation [J].
Ballar, Petek ;
Zhong, Yongwang ;
Nagahama, Masami ;
Tagaya, Mitsuo ;
Shen, Yuxian ;
Fang, Shengyun .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2007, 282 (47) :33908-33914
[9]   Hrd1p/Der3p is a membrane-anchored ubiquitin ligase required for ER-associated degradation [J].
Bays, NW ;
Gardner, RG ;
Seelig, LP ;
Joazeiro, CA ;
Hampton, RY .
NATURE CELL BIOLOGY, 2001, 3 (01) :24-29
[10]   HRD4/NPL4 is required for the proteasomal processing of ubiquitinated ER proteins [J].
Bays, NW ;
Wilhovsky, SK ;
Goradia, A ;
Hodgkiss-Harlow, K ;
Hampton, RY .
MOLECULAR BIOLOGY OF THE CELL, 2001, 12 (12) :4114-4128