title: Taking LSD 1 to a new high.
abstract: Histone modifications mediate changes in gene expression by altering the underlying chromatin structure or by serving as a binding platform to recruit other proteins. One such modification, histone methylation, was thought to be irreversible until last year when Shi and co-workers broke new ground with their discovery of a lysine-specific histone demethylase (LSD 1). They showed that LSD 1, a nuclear amine oxidase homolog, is a bona fide histone H3 lysine 4 demethylase (Shi et al., 2004). Now, a new study from published in a recent issue of Molecular Cell, together with two studies recently published by and in Nature, reveal that LSD 1's specificity and activity is in fact regulated by associated protein cofactors.
authors.affiliation: Laboratory of Chromatin Biology, the Rockerfeller University, New York, NY 10021, USA.
authors.forename: Joanna
authors.initials: J
authors.lastname: Wysocka
authors.forename: Thomas A
authors.initials: TA
authors.lastname: Milne
authors.forename: C David
authors.initials: CD
authors.lastname: Allis
mesh_terms: D002843:Chromatin / Q000378:metabolism; D056466:Histone Demethylases; D006657:Histones / Q000378:metabolism*; D006801:Humans; D008745:Methylation; D008954:Models, Biological; D009707:Nucleosomes / Q000378:metabolism; D010089:Oxidoreductases, N-Demethylating / Q000378:metabolism*
chemical_list: D002843:Chromatin; D006657:Histones; D009707:Nucleosomes; D056466:Histone Demethylases; C495195:KDM1A protein, human; D010089:Oxidoreductases, N-Demethylating