Höhfeld J, Cyr D M, Patterson C
Institut für Zellbiologie, Rheinische Friedrich-Wilhelms-Universität Bonn, Ulrich-Haberland-Strasse 61a, D-53121 Bonn, Germany.
EMBO Rep. 2001 Oct;2(10):885-90. doi: 10.1093/embo-reports/kve206.
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.
已知分子伴侣可促进细胞内蛋白质折叠。它们结合未折叠的蛋白质，并与调节分子伴侣对其底物亲和力的调节辅因子协同调控折叠过程。然而，并非每次蛋白质折叠尝试都能成功，分子伴侣可将错误折叠的蛋白质导向细胞降解机制进行破坏。因此，蛋白质质量控制似乎涉及分子伴侣与能量依赖性蛋白酶之间的密切合作。到目前为止，这种相互作用的分子机制在很大程度上仍是个谜。在此，我们提出了一个关于真核生物Hsp70和Hsp90伴侣系统在蛋白质折叠和蛋白质降解过程中调控的新概念。
