Lysine-specific demethylase 1A (KDM1A, also termed LSD1) is an epigenetic regulatory enzyme that catalyzes the removal of methyl groups from lysine residues 4 and 9 on histone H3 (H3K4 and H3K9, respectively). KDM1A activity has been linked to several processes involved in both normal cell function and disease states, including neuronal development, cancer progression and metastasis, and viral pathogenesis. In each of these biological contexts, KDM1A participates in discreet, multiprotein complexes that direct its activity toward specific substrates to produce unique transcriptional outcomes. Although pan-inhibition strategies have greatly enhanced our understanding of KDM1A biology, there remains a lack of tools to probe the protein-protein interactions that govern KDM1A function. We present here our efforts towards developing molecules capable of disrupting these interactions. With these tools we hope to examining the essentiality of KDM1A as a catalytic subunit within larger complexes and potentially identify novel therapeutic targets.

Targeting protein-protein interactions for disruption of KDM1A (LSD1) complexes

251st National Meeting (2016)

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