Background:The levels of the KDM4B histone demethylase are elevated in different types of cancer cells, and its depletion suppresses tumor formation. Results: Pharmacological inhibition of Hsp90 promotes ubiquitin-dependent proteasomal degradation of KDM4B, hence altering the histone code. Conclusion: KDM4B is a bona fide client protein of Hsp90. Significance: Hsp90 inhibitors may be useful for the treatment of tumors driven by KDM4B overexpression.
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