The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability.

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. Thes

SUBMITTER: Wu Y 

PROVIDER: S-EPMC7333477 | biostudies-literature | 2020 Jul

REPOSITORIES: biostudies-literature