HSP90AB1: Helping the good and the bad.
HSP90AB1: Helping the good and the bad.
复制标题
DOI：
10.1016/j.gene.2015.08.063
复制
发表时间：
2016-01-10
期刊：
影响因子：
3.5
通讯作者：
Fitze G
中科院分区：
文献类型：
--
作者：
Haase M;Fitze G
HSP90AB1（热休克蛋白90kda α， B类，成员1），也称为HSP90beta，是热休克蛋白大家族的一员，具有分子伴侣的功能。伴侣蛋白通过与客户蛋白结合，支持适当的蛋白质折叠并维持蛋白质的稳定性，特别是在暴露于各种细胞应激后。客户蛋白属于多种蛋白家族，包括激酶、泛素连接酶和转录因子。HSP90蛋白作为二聚体，在共同伴侣的帮助下结合客户。伴蛋白影响HSP90的许多功能，包括客户端结合、ATP酶活性或ATP结合。热休克蛋白是大规模细胞过程所必需的，因此对细胞存活至关重要。由于客户蛋白可能是突变蛋白，在没有伴侣的帮助下会被降解，因此热休克蛋白还可以促进肿瘤的形成和癌细胞的增殖。因此，它们也是癌症治疗新方法的目标。本文将对HSP90AB1的最新研究进行综述，并尽可能将其与同源物HSP90AA1进行比较。
HSP90AB1 (heat shock protein 90 kDA alpha, class B, member 1), also known as HSP90beta, is a member of the large family of HSPs which function as molecular chaperones. Chaperones, by binding to client proteins, support proper protein folding and maintain protein stability, especially after exposure to various kinds of cellular stress. Client proteins belong to various protein families including kinases, ubiquitin ligases and transcription factors. HSP90 proteins act as dimers and bind clients with the help of co-chaperones. The cochaperones influence many functions including client binding, ATPase activity or ATP binding of HSP90. HSPs are necessary for a large scale of cellular processes and therefore essential for cell survival. Since client proteins can be mutant proteins that would be degraded without the help of chaperones, HSPs also promote tumor formation and cancer cell proliferation. As such, they are also targets for new therapeutic approaches in cancer treatment. This review focuses on recent studies on HSP90AB1, if possible in comparison with its close homologue HSP90AA1.
登录
查看更多内容
影响因子：
56.9
作者：
Bose, S;Weikl, T;Buchner, J
通讯作者：
Buchner, J
影响因子：
4.3
作者：
Aressy, Bernadette;Jullien, Denis;Ducommun, Bernard
通讯作者：
Ducommun, Bernard
影响因子：
3.7
作者：
Boltze, C;Lehnert, H;Roessner, A
通讯作者：
Roessner, A
影响因子：
4.8
作者：
Carrello, A;Ingley, E;Ratajczak, T
通讯作者：
Ratajczak, T
影响因子：
3.5
作者：
Chen, Huaqun;Wu, Yifan;Yin, Zhimin
通讯作者：
Yin, Zhimin