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- W2000889104 abstract "Heat shock protein 90 (Hsp90) is a molecular chaperone required for the conformational maturation and function of certain signaling proteins. Hsp90 inhibitors cause the inactivation, destabilization and eventual degradation of Hsp90 client proteins through occupying the ATP/ADP binding pocket of Hsp90. In the present study, we found that Hsp90 interacted with MEKK3 in HEK293 cells. Hsp90 inhibitors reduced the level of endogenous MEKK3 in time- and dose-dependent manners, and this decrease was reversed by Hsp90 overexpression. In addition, Hsp90 RNAi destabilized MEKK3. A selective inhibitor of Hsp90, geldanamycin (GA), shortened MEKK3 half-life, and induced ubiquitination and proteasomal degradation of MEKK3. These results strongly suggested that Hsp90 could work as the molecular chaperone of MEKK3." @default.
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- W2000889104 date "2009-01-01" @default.
- W2000889104 modified "2023-09-27" @default.
- W2000889104 title "Heat shock protein 90 regulates the stability of MEKK3 in HEK293 cells" @default.
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- W2000889104 doi "https://doi.org/10.1016/j.cellimm.2009.05.012" @default.
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