Abstract 1918 Functional Analysis of the Lysine Specific Demethylase 1 (LSD1) Enzyme Complex with EWS-FLI1 protein constructs

Lysine specific demethylase 1 (LSD1) is an essential epigenetic regulator involved in chromatin remodeling that requires the co-repressor element-1 silencing transcription factor (CoREST) to catalyze the removal of mono- and dimethyl groups from histone 3 at lysine positions 4 and 9 (H3K4/9). LSD1 interacts with >100 proteins and plays a critical role in embryogenesis. Importantly, its misregulation is associated with cancer progression, including Ewing sarcoma. To study the biochemical properties and potential therapeutic relevance of LSD1, we overexpressed a form of LSD1 that lacks the N-terminus region (ΔN LSD1) and is in complex with CoREST.