From the cradle to the grave:: molecular chaperones that may choose between folding and degradation
From the cradle to the grave:: molecular chaperones that may choose between folding and degradation
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DOI：
10.1093/embo-reports/kve206
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发表时间：
2001-10-01
期刊：
影响因子：
7.7
通讯作者：
Patterson, C
中科院分区：
文献类型：
--
作者：
Höhfeld, J;Cyr, DM;Patterson, C
已知分子伴侣促进细胞蛋白质折叠。它们结合非天然蛋白质，并与调节伴侣对底物亲和力的调节辅因子一起协调折叠过程。然而，并不是每一次折叠蛋白质的尝试都是成功的，伴侣蛋白可以将错误折叠的蛋白质引导到细胞降解机制中进行破坏。因此，蛋白质质量控制似乎涉及分子伴侣和能量依赖性蛋白酶之间的密切合作。到目前为止，这种相互作用背后的分子机制在很大程度上还是个谜。在这里，我们提出了真核Hsp70和Hsp90伴侣系统在蛋白质折叠和蛋白质降解过程中的调控的新概念。
Molecular chaperones are known to facilitate cellular protein folding. They bind non-native proteins and orchestrate the folding process in conjunction with regulatory cofactors that modulate the affinity of the chaperone for its substrate. However, not every attempt to fold a protein is successful and chaperones can direct misfolded proteins to the cellular degradation machinery for destruction. Protein quality control thus appears to involve close cooperation between molecular chaperones and energy-dependent proteases. Molecular mechanisms underlying this interplay have been largely enigmatic so far. Here we present a novel concept for the regulation of the eukaryotic Hsp70 and Hsp90 chaperone systems during protein folding and protein degradation.