How Do J-Proteins Get Hsp70 to Do So Many Different Things?
How Do J-Proteins Get Hsp70 to Do So Many Different Things?
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DOI：
10.1016/j.tibs.2017.02.007
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发表时间：
2017-05
影响因子：
13.8
通讯作者：
Marszalek J
中科院分区：
文献类型：
--
作者：
Craig EA;Marszalek J
Hsp70 分子伴侣机制通过促进蛋白质折叠、解聚和重塑，在多种基本生物过程中发挥着关键作用。 Hsp70 的专性 J 蛋白共伴侣在很大程度上推动了这种非凡的多功能性，大多数 Hsp70 具有多个 J 蛋白伴侣。最近的数据表明，J 蛋白驱动的多功能性很大程度上归因于细胞内的精确定位和底物蛋白结合的特异性。然而，这种相对简单的观点掩盖了 J 蛋白功能的复杂性。 J 蛋白与 Hsp70 和其他分子伴侣相互作用以及整合到更广泛的细胞网络中的例子不断涌现。这些相互作用以关键方式微调 Hsp70 参与不同细胞过程的能力。
Hsp70 chaperone machineries play pivotal roles in a wide array of fundamental biological processes, through their facilitation of protein folding, disaggregation and remodeling. Hsp70’s obligate J-protein co-chaperones drive much of this remarkable multi-functionality, with most Hsp70s having multiple J-protein partners. Recent data suggest that J-protein-driven versatility is substantially due to precise localization within the cell and specificity of substrate protein binding. However, this relatively simple view belies the intricacy of J-protein function. Examples are emerging of J-protein interactions with Hsp70 and other chaperones, as well as integration into broader cellular networks. These interactions fine-tune, in critical ways, the ability of Hsp70 to participate in diverse cellular processes.