Lysine-specific histone demethylase
From Proteopedia
Contents |
Function
Lysine-specific histone demethylase 1 (LSD1) is a flavin-dependent oxidase that catalyzes the removal of methyl groups from mono- and dimethylated lysine 4 of histone H3. LSD1 is a nuclear homolog of amine oxidase. It functions as histone demethylase and transcriptional corepressor. LSD1 demethylation occurs via a reaction which produces formaldehyde. LSD1 is a component of transcriptional corepressor complex which also contains CoREST (corepressor of element-1-silencing transcription factor)[1].
Relevance
LSD1 is a potential anti-tumor drug target since it inhibits the tumor suppressor p53[2].
3D structures of lysine-specific histone demethylase 1
Updated on 13-April-2016
References
- ↑ Chen Y, Jie W, Yan W, Zhou K, Xiao Y. Lysine-specific histone demethylase 1 (LSD1): A potential molecular target for tumor therapy. Crit Rev Eukaryot Gene Expr. 2012;22(1):53-9. PMID:22339659
- ↑ Pollock JA, Larrea MD, Jasper JS, McDonnell DP, McCafferty DG. Lysine-specific histone demethylase 1 inhibitors control breast cancer proliferation in ERalpha-dependent and -independent manners. ACS Chem Biol. 2012 Jul 20;7(7):1221-31. doi: 10.1021/cb300108c. Epub 2012 May, 10. PMID:22533360 doi:http://dx.doi.org/10.1021/cb300108c
Proteopedia Page Contributors and Editors (what is this?)
Michal Harel, Alexander Berchansky, Joel L. Sussman, Jaime Prilusky
