The molecular chaperone Hsp90 maintains Golgi organization and vesicular trafficking by regulating microtubule stability.
J Mol Cell Biol
; 12(6): 448-461, 2020 07 03.
Article
in En
| MEDLINE
| ID: mdl-31560394
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.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
HSP90 Heat-Shock Proteins
/
Transport Vesicles
/
Golgi Apparatus
/
Microtubules
Limits:
Humans
Language:
En
Journal:
J Mol Cell Biol
Journal subject:
BIOLOGIA MOLECULAR
Year:
2020
Type:
Article
Affiliation country:
China