Pathways of chaperone-mediated protein folding in the cytosol

被引:902
作者
Young, JC
Agashe, VR
Siegers, K
Hartl, FU
机构
[1] Max Planck Inst Biochem, Dept Cellular Biochem, D-82152 Martinsried, Germany
[2] McGill Univ, Dept Biochem, Montreal, PQ H3C 1Y6, Canada
关键词
D O I
10.1038/nrm1492
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
Cells are faced with the task of folding thousands of different polypeptides into a wide range of conformations. For many proteins, the folding process requires the action of molecular chaperones. In the cytosol of prokaryotic and eukaryotic cells, molecular chaperones of different structural classes form a network of pathways that can handle substrate polypeptides from the point of initial synthesis on ribosomes to the final stages of folding.
引用
收藏
页码:781 / 791
页数:11
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