Protein Folding and Quality Control in the ER

被引:240
|
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
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 50 条
  • [41] Orchestration of secretory protein folding by ER chaperones
    Gidalevitz, Tali
    Stevens, Fred
    Argon, Yair
    BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH, 2013, 1833 (11): : 2410 - 2424
  • [42] Protein folding during cotranslational translocation in the ER
    Kowarik, MT
    Martoglio, B
    Kung, S
    Helenius, A
    MOLECULAR BIOLOGY OF THE CELL, 2001, 12 : 480A - 480A
  • [43] The Relationship between ER Stress and Protein Quality Control at the Translocon
    Broshar, Courtney
    Buchanan, Bryce
    Mehrtash, Adrian
    Runnebohm, Avery
    Snow, Brian
    Scanameo, Laura
    Hochstrasser, Mark
    Rubenstein, Eric
    FASEB JOURNAL, 2020, 34
  • [44] ER-associated degradation: Protein quality control and beyond
    Ruggiano, Annamaria
    Foresti, Ombretta
    Carvalho, Pedro
    JOURNAL OF CELL BIOLOGY, 2014, 204 (06): : 868 - 878
  • [45] The endoplasmic reticulum: integration of protein folding, quality control, signaling and degradation
    Chevet, E
    Cameron, PH
    Pelletier, MF
    Thomas, DY
    Bergeron, JJM
    CURRENT OPINION IN STRUCTURAL BIOLOGY, 2001, 11 (01) : 120 - 124
  • [46] Quality control in the ER
    Wilson, JDK
    NATURE IMMUNOLOGY, 2004, 5 (07) : 693 - 693
  • [47] The role of chaperone-assisted folding and quality control in inborn errors of metabolism: Protein folding disorders
    Gregersen, N
    Bross, P
    Andresen, BS
    Pedersen, CB
    Corydon, TJ
    Bolund, L
    JOURNAL OF INHERITED METABOLIC DISEASE, 2001, 24 (02) : 189 - 212
  • [48] The expanding role of the ER translocon in membrane protein folding
    Skach, William R.
    JOURNAL OF CELL BIOLOGY, 2007, 179 (07): : 1333 - 1335
  • [49] Protein folding stress in neurodegenerative diseases: a glimpse into the ER
    Matus, Soledad
    Glimcher, Laurie H.
    Hetz, Claudio
    CURRENT OPINION IN CELL BIOLOGY, 2011, 23 (02) : 239 - 252
  • [50] Integration of ER protein quality-control mechanisms defines ß cell function and ER architecture
    Shrestha, Neha
    Torres, Mauricio
    Zhang, Jason
    Lu, You
    Haataja, Leena
    Reinert, Rachel B.
    Knupp, Jeffrey
    Chen, Yu-Jie
    Parlakgul, Gunes
    Arruda, Ana Paula
    Tsai, Billy
    Arvan, Peter
    Qi, Ling
    JOURNAL OF CLINICAL INVESTIGATION, 2023, 133 (01):