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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. 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.

SUBMITTER: Wu Y

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

REPOSITORIES: biostudies-literature

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

Wu Yuan Y Ding Yubo Y Zheng Xiudan X Liao Kan K

Journal of molecular cell biology 20200701 6

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 st ...[more]

PMID: 31560394

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Project description:The ability to survive stress conditions is important for every living cell. Some stresses can affect not only current cell well-being, but may have far-reaching consequences. Uncurbed oxidative stress can cause DNA damage and the decrease in cell survival and/or increase in mutation rate. Some substances generating oxidative damage in the cell act mainly on DNA. Radiomimetic zeocin is a chemoenzyme that causes oxidative damage in DNA, inducing predominantly single or double strand breaks. Such lesions can subsequently lead to chromosomal rearrangements in genomic DNA, especially in diploid cells in which each sequence has its duplicate in the homologous chromosome. In a global screen for mutants oversensitive to zeocin, we selected 136 genes whose deletion causes the decrease in survival of diploid Saccharomyces cerevisiae cells exposed to this compound. The screen revealed numerous genes connected with stress response, including response to DNA damage stimulus; DNA repair genes, especially connected with homologous recombination and telomere maintenance; genes involved in cell cycle progression, chiefly in control of cell divisions checkpoints, both meiotic and mitotic; and genes involved in remodeling of chromatin. Notably, our screen also demonstrated the involvement of vesicular trafficking system in cell protection against DNA damage. Presented data imply vesicular system in various pathways of cell protection from zeocin-dependent damage, including the role in detoxification and probably more direct role in genome maintenance processes. We show, that cells with vesicular trafficking dysfunction are unable to repair zeocin induced damage, accumulate Rad52 foci and frequently possess an atypical DNA content. Therefore, we postulate that functional vesicular trafficking is crucial for sustaining integral genome. We believe that numerous new genes implicated in genome maintenance after genotoxic oxidative stress, together with newly discovered vesicular trafficking link to genome integrity, will help revealing novel molecular processes involved in the genome stability of diploid cells.

Dataset Information

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

Publications

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

Similar Datasets

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