Visualizing the histone code on LSD1.
In this issue, Garcia-Bassets et al. (2007) show that spurious transcriptional activation by unliganded nuclear receptors is inhibited by histone lysine methylation. This inhibitory histone modification code is efficiently countered by the ligand-dependent recruitment of histone lysine demethylases, including lysine-specific demethylase 1 (LSD1), which appear to be used for this purpose by a number of signal-regulated transcriptional activators.
Gamble
Matthew J
MJ
Department of Molecular Biology and Genetics, 465 Biotechnology Building, Cornell University, Ithaca, NY 14853, USA.
Kraus
W Lee
WL
D045744:Cell Line, Tumor; D047628:Estrogen Receptor alpha / Q000378:metabolism*; D005786:Gene Expression Regulation; D042421:Histone Code; D056466:Histone Demethylases; D011495:Histone-Lysine N-Methyltransferase / Q000235:genetics / Q000378:metabolism; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008024:Ligands; D008745:Methylation; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*; D015533:Transcriptional Activation
D047628:Estrogen Receptor alpha; D006657:Histones; D008024:Ligands; D056466:Histone Demethylases; C495195:KDM1A protein, human; D010089:Oxidoreductases, N-Demethylating; D011495:Histone-Lysine N-Methyltransferase