The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability
The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability
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分子伴侣 Hsp90 通过调节微管稳定性维持高尔基体组织和囊泡运输
DOI:
10.1093/jmcb/mjz093
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发表时间:
2019-09
影响因子:
5.5
通讯作者:
Kan Liao
中科院分区:
文献类型:
--
作者:
Yuan;Yubo Ding;Xiudan Zheng;Kan Liao
Abstract Hsp90 is an abundant and special molecular chaperone considered to be the regulator of many transcription factors and signaling kinases. Its high abundance is indicative of its involvement in some more fundamental processes. In this study, we provide evidence that Hsp90 is required for microtubule stabilization, Golgi organization, and vesicular trafficking. We showed that Hsp90 is bound to microtubule-associated protein 4 (MAP4), which is essential for maintaining microtubule acetylation and stabilization. Hsp90 depletion led to the decrease in MAP4, causing microtubule deacetylation and destabilization. Furthermore, in Hsp90-depleted cells, the Golgi apparatus was fragmented and anterograde vesicle trafficking was impaired, with phenotypes similar to those induced by silencing MAP4. These disruptive effects of Hsp90 depletion could be rescued by the expression of exogenous MAP4 or the treatment of trichostatin A that increases microtubule acetylation as well as stability. Thus, microtubule stability is an essential cellular event regulated by Hsp90.
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影响因子:
5.5
作者:
Yuan Wu;Xiudan Zheng;Yubo Ding;Min Zhou;Zhuang Wei;Tao Liu;Kan Liao
通讯作者:
Kan Liao
影响因子:
4
作者:
P. Csermely;T. Schnaider;Z. Prohászka;G. Nardai
通讯作者:
P. Csermely;T. Schnaider;Z. Prohászka;G. Nardai
影响因子:
7.4
作者:
Zhang Fengqiu;Huang Qing;Yan Jingwen;Zhang Xin;Li Jianxin
通讯作者:
Li Jianxin
影响因子:
4.8
作者:
Giustiniani, Julien;Daire, Vanessa;Baillet, Anita
通讯作者:
Baillet, Anita
影响因子:
11.4
作者:
Bravo-Cordero, Jose J.;Marrero-Diaz, Raquel;Montoya, Maria C.
通讯作者:
Montoya, Maria C.