Disulfide Bond Formation in the Mammalian Endoplasmic Reticulum

被引:78
作者
Bulleid, Neil J. [1 ]
机构
[1] Univ Glasgow, Inst Mol Cellular & Syst Biol, Coll Med Vet & Life Sci, Glasgow G12 8QQ, Lanark, Scotland
来源
COLD SPRING HARBOR PERSPECTIVES IN BIOLOGY | 2012年 / 4卷 / 11期
基金
英国惠康基金;
关键词
HUMAN PROTEIN; SULFHYDRYL OXIDASE; PEROXIREDOXIN-IV; TRANSMEMBRANE PROTEIN; REDOX REGULATION; STRUCTURAL BASIS; HUMAN-CELLS; OXIDATION; ISOMERASE; GLUTATHIONE;
D O I
10.1101/cshperspect.a013219
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The formation of disulfide bonds between cysteine residues occurs during the folding of many proteins that enter the secretory pathway. As the polypeptide chain collapses, cysteines brought into proximity can form covalent linkages during a process catalyzed by members of the protein disulfide isomerase family. There are multiple pathways in mammalian cells to ensure disulfides are introduced into proteins. Common requirements for this process include a disulfide exchange protein and a protein oxidase capable of forming disulfides de novo. In addition, any incorrect disulfides formed during the normal folding pathway are removed in a process involving disulfide exchange. The pathway for the reduction of disulfides remains poorly characterized. This work will cover the current knowledge in the field and discuss areas for future investigation.
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页数:12
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