A selective jumonji H3K27 demethylase inhibitor modulates the proinflammatory macrophage response.

ABSTRACT: The jumonji (JMJ) family of histone demethylases are Fe2+- and α-ketoglutarate-dependent oxygenases that are essential components of regulatory transcriptional chromatin complexes. These enzymes demethylate lysine residues in histones in a methylation-state and sequence-specific context. Considerable effort has been devoted to gaining a mechanistic understanding of the roles of histone lysine demethylases in eukaryotic transcription, genome integrity and epigenetic inheritance, as well as in development, physiology and disease. However, because of the absence of any selective inhibitors, the relevance of the demethylase activity of JMJ enzymes in regulating cellular responses remains poorly understood. Here we present a structure-guided small-molecule and chemoproteomics approach to elucid

SUBMITTER: Kruidenier L 

PROVIDER: S-EPMC4691848 | biostudies-literature | 2012 Aug

REPOSITORIES: biostudies-literature