Histone Demethylation Mediated by the Nuclear Amine Oxidase Homolog LSD1

  • Yujiang Shi, 1 Fei Lan, 1 Caitlin Matson 1
  • Peter Mulligan 1
  • Johnathan R. Whetstine 1
  • et al.
Citations of this article
Mendeley users who have this article in their library.
Get full text


Posttranslational modifications of histone N-terminal tails impact chromatin structure and gene transcrip- tion. While the extent of histone acetylation is deter- mined by both acetyltransferases and deacetylases, it has been unclear whether histone methylation is also regulated by enzymes with opposing activities. Here, we provide evidence that LSD1 (KIAA0601), a nuclear homolog of amine oxidases, functions as a histone demethylase and transcriptional corepressor. LSD1 specifically demethylates histone H3 lysine 4, which is linked to active transcription. Lysine demeth- ylation occurs via an oxidation reaction that generates formaldehyde. Importantly, RNAi inhibition of LSD1 causes an increase in H3 lysine 4 methylation and concomitant derepression of target genes, suggesting that LSD1 represses transcription via histone demeth- ylation. The results thus identify a histone demethylase conserved from S. pombe to human and reveal dy- namic regulation of histone methylation by both his- tone methylases and demethylases.




Yujiang Shi, 1 Fei Lan, 1 Caitlin Matson, 1, Peter Mulligan, 1, Johnathan R. Whetstine, 1, Philip A. Cole, 2, Robert A. Casero, 3, & and Yang Shi1, *. (2004). Histone Demethylation Mediated by the Nuclear Amine Oxidase Homolog LSD1. Cell, 119(4), 941–953. https://doi.org/10.1039/FT9949000533

Register to see more suggestions

Mendeley helps you to discover research relevant for your work.

Already have an account?

Save time finding and organizing research with Mendeley

Sign up for free