Formation, isomerisation and reduction of disulphide bonds during protein quality control in the endoplasmic reticulum

被引：71
作者：
Fassio, A
Sitia, R
机构：
[1] DiBiT HSR, I-20132 Milan, Italy
[2] Univ Vita Salute San Raffaele, I-20132 Milan, Italy
来源：
HISTOCHEMISTRY AND CELL BIOLOGY | 2002年 / 117卷 / 02期
关键词：
degradation; endoplasmic reticulum; membrane insertion; oxidative protein folding; redox;
D O I：
10.1007/s00418-001-0364-0
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Efficient protein folding and quality control in the endoplasmic reticulum (ER) require that disulphide bonds are formed in nascent proteins, isomerised during assisted folding and reduced in terminally misfolded molecules. Recent findings in yeast and mammalian cells indicate that specific protein-protein interactions underlie redox control in the ER, allowing these competing reactions to occur simultaneously during protein quality control.
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收藏
页码：151 / 157
页数：7
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