Abstract Chaperones of the 70 kDa heat shock protein (Hsp70) superfamily are key components of the cellular proteostasis system. Together with its co-chaperones, Hsp70 forms proteostasis subsystems that antagonize protein damage during physiological and stress conditions. This function stems from highly regulated binding and release cycles of protein substrates, which results in a flow of unfolded, partially folded and misfolded species through the Hsp70 subsystem. Specific factors control how Hsp70 makes decisions regarding folding and degradation fates of the substrate proteins. In this review, we summarize how the flow of Hsp70 substrates is controlled in the cell with special emphasis on recent advances regarding substrate release mechanisms.

中文翻译：

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Hsp70介导的质量控制：我应该留下还是我应该去？

摘要 70 kDa 热休克蛋白 (Hsp70) 超家族的分子伴侣是细胞蛋白质稳态系统的关键组成部分。Hsp70 与其共同伴侣一起形成蛋白质稳态子系统，在生理和压力条件下对抗蛋白质损伤。这种功能源于高度调节的蛋白质底物结合和释放周期，这导致未折叠、部分折叠和错误折叠的物种通过 Hsp70 子系统流动。特定因素控制 Hsp70 如何决定底物蛋白质的折叠和降解命运。在这篇综述中，我们总结了 Hsp70 底物在细胞中的流动是如何控制的，并特别强调了有关底物释放机制的最新进展。