GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones.
GrpE, Hsp110/Grp170, HspBP1/Sil1 and BAG domain proteins: nucleotide exchange factors for Hsp70 molecular chaperones.
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DOI：
10.1007/978-3-319-11731-7_1
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发表时间：
2015-01-01
影响因子：
--
通讯作者：
Verghese, Jacob
中科院分区：
文献类型：
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作者：
Bracher, Andreas;Verghese, Jacob
Hsp 70家族的分子伴侣是细胞蛋白质折叠机制的关键组分。底物折叠通过ATP结合、水解和释放的反复循环来完成。Hsp 70的ATP酶活性受两类主要的辅助分子伴侣的调节：J结构域蛋白刺激Hsp 70的ATP酶水解，而核苷酸交换因子（NEF）促进其从ADP结合状态转化为ATP结合状态，从而关闭伴侣折叠循环。从发现原型细菌NEF GrpE开始，已经鉴定了大量多样性的Hsp 70核苷酸交换因子，将Hsp 70连接到真核细胞中的众多细胞过程。本文综述了Hsp 110/Grp 170、HspBP 1/Sil 1和BAG结构域蛋白家族的核苷酸交换因子的结构和功能，并讨论了这些辅伴侣分子如何将蛋白质折叠与质量控制和降解途径联系起来。
Molecular chaperones of the Hsp70 family are key components of the cellular protein folding machinery. Substrate folding is accomplished by iterative cycles of ATP binding, hydrolysis and release. The ATPase activity of Hsp70 is regulated by two main classes of cochaperones: J-domain proteins stimulate ATPase hydrolysis by Hsp70, while nucleotide exchange factors (NEF) facilitate its conversion from the ADP-bound to the ATP-bound state, thus closing the chaperone folding cycle. Beginning with the discovery of the prototypical bacterial NEF GrpE, a large diversity of Hsp70 nucleotide exchange factors has been identified, connecting Hsp70 to a multitude of cellular processes in the eukaryotic cell. Here we review recent advances towards structure and function of nucleotide exchange factors from the Hsp110/Grp170, HspBP1/Sil1 and BAG domain protein families and discuss how these cochaperones connect protein folding with quality control and degradation pathways.