Ben-Khoud Yassin, Chen Chao-Sheng, Ali Maruf M U
Department of Life Sciences, Imperial College London, London, United Kingdom.
Front Mol Biosci. 2023 Mar 16;10:1155784. doi: 10.3389/fmolb.2023.1155784. eCollection 2023.
Hsp70 molecular chaperones are essential components for maintaining protein homeostasis within cells. They interact with substrate or client proteins in a well characterised fashion that is regulated by ATP and supported by co-chaperones. In eukaryotes there is a vast array of Hsp70 isoforms that may facilitate adaption to a particular cellular compartment and distinct biological role. Emerging data indicate a novel type of interaction between Hsp70 and client protein that does not fit with the classical Hsp70 ATP regulated substrate mechanism. In this review, we highlight Hsp70 ATPase domain interactions with binding partners from various biological systems that we refer to as sp70 TPase lternative inding proteins or HAAB proteins. We identify common mechanistic features that may define how Hsp70 operates when associating with proteins in this alternative HAAB mode of action.
热休克蛋白70（Hsp70）分子伴侣是维持细胞内蛋白质稳态的重要组成部分。它们以一种由ATP调节并由共伴侣支持的、特征明确的方式与底物或客户蛋白相互作用。在真核生物中，有大量的Hsp70亚型，它们可能有助于适应特定的细胞区室和独特的生物学作用。新出现的数据表明，Hsp70与客户蛋白之间存在一种新型相互作用，这种相互作用不符合经典的Hsp70 ATP调节底物机制。在本综述中，我们重点介绍了Hsp70 ATP酶结构域与来自各种生物系统的结合伙伴之间的相互作用，我们将这些结合伙伴称为Hsp70 ATP酶替代结合蛋白或HAAB蛋白。我们确定了一些共同的机制特征，这些特征可能定义了Hsp70在以这种替代的HAAB作用模式与蛋白质结合时的运作方式。
