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• W3178589622 endingPage "119096" @default.
• W3178589622 startingPage "119096" @default.
• W3178589622 abstract "Heat shock protein 90 (HSP90) is a highly conserved molecular chaperone that plays a pivotal role in folding, activating and assembling a variety of client proteins. In addition, HSP90 has recently emerged as a crucial regulator of vesicular transport of cellular proteins. In our previous study, we revealed Rab11b negatively regulated osteoclastogenesis by promoting the lysosomal proteolysis of c-fms and RANK surface receptors via the axis of early endosome-late endosome-lysosomes. In this study, using an in vitro model of osteoclasts differentiated from murine macrophage-like RAW-D cells, we revealed that Rab11b interacted with both HSP90 isoforms, HSP90 alpha (HSP90α) and HSP90 beta (HSP90β), suggesting that Rab11b is an HSP90 client. Using at specific blocker for HSP90 ATPase activity, 17-allylamino-demethoxygeldanamycin (17-AAG), we found that the HSP90 ATPase domain is indispensable for maintaining the interaction between HSP90 and Rab11b in osteoclasts. Nonetheless, its ATPase activity is not required for regulating the turnover of endogenous Rab11b. Interestingly, blocking the interaction between HSP90 and Rab11b by either HSP90-targeting small interfering RNA (siHSP90) or 17-AAG abrogated the inhibitory effects of Rab11b on osteoclastogenesis by suppressing the Rab11b-mediated transport of c-fms and RANK surface receptors to lysosomes via the axis of early endosome-late endosome-lysosomes, alleviating the Rab11b-mediated proteolysis of these surface receptors in osteoclasts. Based on our observations, we propose a HSP90/Rab11b-mediated regulatory mechanism for osteoclastogenesis by directly modulating the c-fms and RANK surface receptors in osteoclasts, thereby contributing to the maintenance of bone homeostasis. • Rab11b interacts with HSP90 in osteoclasts • The ATPase domain of HSP90 is essential for the maintenance of the interaction of HSP90 with Rab11b in osteoclasts. • HSP90 directly regulates Rab11b-mediated vesicular transport of c-fms and RANK surface receptors in osteoclasts." @default.
• W3178589622 created "2021-07-19" @default.
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• W3178589622 date "2021-09-01" @default.
• W3178589622 modified "2023-10-16" @default.
• W3178589622 title "A novel role of HSP90 in regulating osteoclastogenesis by abrogating Rab11b-driven transport" @default.
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• W3178589622 doi "https://doi.org/10.1016/j.bbamcr.2021.119096" @default.
• W3178589622 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/34242681" @default.
• W3178589622 hasPublicationYear "2021" @default.
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