Detecting Posttranslational Modifications of Hsp90.
Detecting Posttranslational Modifications of Hsp90.
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检测 Hsp90 的翻译后修饰。
DOI：
10.1007/978-1-4939-7477-1_16
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发表时间：
2018
期刊：
影响因子：
--
通讯作者：
Mollapour,Mehdi
中科院分区：
文献类型：
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作者：
Sager,RebeccaA;Woodford,MarkR;Neckers,Len;Mollapour,Mehdi
分子伴侣热休克蛋白90(Hsp90)在真核生物中是必不可少的。HSP90伴侣蛋白是多步致癌的重要决定因素。Hsp90的伴侣功能与其结合和水解三磷酸腺苷的能力有关。辅伴侣和翻译后修饰(磷酸化、SUMO化和泛素化)对于其稳定性和ATPase活性的调节是重要的。哺乳动物细胞和酵母细胞均可用于表达和纯化Hsp90，也可通过免疫印迹法检测其翻译后修饰。
The molecular chaperone Heat Shock Protein 90 (Hsp90) is essential in eukaryotes. Hsp90 chaperones proteins that are important determinants of multistep carcinogenesis. The chaperone function of Hsp90 is linked to its ability to bind and hydrolyze ATP. Co-chaperones as well as posttranslational modifications (phosphorylation, SUMOylation, and ubiquitination) are important for its stability and regulation of the ATPase activity. Both mammalian and yeast cells can be used to express and purify Hsp90 and also detect its posttranslational modifications by immunoblotting.