Profiling Inhibitor Scaffolds for the Cancer Target Jumonji-C Domain-Containing Protein 6.

ABSTRACT: The human 2-oxoglutarate-dependent oxygenase Jumonji-C domain-containing protein 6 (JMJD6) catalyzes post-translational C-5 lysyl residue hydroxylation in multiple proteins. Aberrant JMJD6 catalysis is associated with the upregulation of androgen receptor splice variant 7 (AR-V7), which confers resistance towards antiandrogens used for prostate cancer treatment; JMJD6 is thus a promising cancer target. To date, few small-molecule JMJD6 inhibitors are reported, likely in part reflecting a lack of robust assays to monitor effects of small molecules on catalysis by isolated JMJD6. The use of solid-phase extraction coupled to mass spectrometry assays is described to screen scaffolds for the development of selective JMJD6 inhibitors. The results reveal that the reported JMJD6 inhibitors WL12, S

SUBMITTER: Corner TP 

PROVIDER: S-EPMC12677844 | biostudies-literature | 2025 Nov

REPOSITORIES: biostudies-literature