共 55 条
Ero1 and redox homeostasis in the endoplasmic reticulum
被引:235
作者:
Sevier, Carolyn S.
[1
]
Kaiser, Chris A.
[1
]
机构:
[1] MIT, Dept Biol, Cambridge, MA 02139 USA
来源:
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
|
2008年
/
1783卷
/
04期
关键词:
Ero1;
Ero1p;
flavoprotein;
oxidase;
sulfhydryl oxidase;
chaperone;
disulfide;
thiol;
oxidation;
reduction;
cysteine;
PDI;
pdi1p;
redox;
endoplasmic reticulum;
ER;
protein folding;
oxidative folding;
disulfide bond formation;
glutathione;
reactive oxygen species;
ROS;
oxidative stress;
posttanslational modification;
posttranslation regulation;
D O I:
10.1016/j.bbamcr.2007.12.011
中图分类号:
Q5 [生物化学];
Q7 [分子生物学];
学科分类号:
071010 ;
081704 ;
摘要:
Living cells must be able to respond to physiological and environmental fluctuations that threaten cell function and viability. A cellular event prone to disruption by a wide variety of internal and external perturbations is protein folding. To ensure protein folding can proceed under a range of conditions, the cell has evolved transcriptional, translational, and posttranslational signaling pathways to maintain folding homeostasis during cell stress. This review will focus on oxidative protein folding in the endoplasmic reticulum (ER) and will discuss the features of the main facilitator of biosynthetic disulfide bond formation, Ero I. Ero I plays an essential role in setting the redox potential in the ER and regulation of Ero1 activity is central to maintain redox homeostasis and proper ER folding activity. (C) 2008 Elsevier B.V. All rights reserved.
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页码:549 / 556
页数:8
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