LSD1s

Lysine-specific demethylase 1, often abbreviated as LSD1, is a protein enzyme belonging to the flavin-dependent oxidase family. It plays a critical role in epigenetic regulation by catalyzing the demethylation of specific lysine residues on histone proteins. This process is fundamental to controlling gene expression, influencing cellular differentiation, proliferation, and development. LSD1 specifically targets the mono- and di-methylated forms of lysine 4 on histone H3 (H3K4me1 and H3K4me2), which are generally associated with transcriptional activation. However, it can also demethylate lysine 9 on histone H3 (H3K9me1 and H3K9me2), which is typically linked to gene silencing. This dual functionality highlights its complex role in orchestrating the epigenetic landscape. LSD1 functions within larger protein complexes, interacting with various co-repressors and co-activators, which dictate its specific regulatory targets and cellular outcomes. Dysregulation of LSD1 activity has been implicated in numerous diseases, including various cancers, neurological disorders, and cardiovascular diseases. Consequently, LSD1 has emerged as a significant target for therapeutic intervention, with several inhibitors currently under development or in clinical trials. Understanding the precise mechanisms of LSD1 action and its involvement in disease pathogenesis is an active area of research.