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Licensed Unlicensed Requires Authentication Published by De Gruyter March 25, 2013

Lysine-specific histone demethylase LSD1 and the dynamic control of chromatin

  • Thomas Rudolph , Stefanie Beuch and Gunter Reuter EMAIL logo
From the journal Biological Chemistry

Abstract

The flavin adenine dinucleotide-dependent amine oxidase LSD1 is the first molecularly defined histone demethylase, which specifically demethylates H3K4me1/me2. The enzyme dynamically controls a large variety of biological processes and is associated with protein complexes controlling transcriptional repression and activation. Molecular analysis of the Drosophila LSD1 homolog revealed new insights into the epigenetic control of heterochromatin formation during early embryogenesis, the establishment of transcriptional gene silencing and the epigenetic mechanisms associated with the maintenance of stem cell identity in primordial germline cells. This review summarizes our recent knowledge about the control of enzymatic activity and molecular function of LSD1 enzyme complexes in different model organisms including Schizosaccharomyces pombe, Drosophila and mammals. Finally, new developments in applied cancer research based on molecular analysis of LSD1 in cancer cells are discussed.


Corresponding author: Gunter Reuter, Institute of Biology, Developmental Genetics, Martin Luther University Halle-Wittenberg, D-06120 Halle, Germany

We thank Gary Sawers for helpful comments on the manuscript. Deutsche Forschungsgemeinschaft (DFG), SFB610, Project C3 supported the work on the LSD1 histone demethylase in the Reuter lab. T.R. is supported by the European Regional Development Fund of the European Commission.

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Received: 2013-1-15
Accepted: 2013-3-21
Published Online: 2013-03-25
Published in Print: 2013-08-01

©2013 by Walter de Gruyter Berlin Boston

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