Inhibition of demethylases by GSK-J1/J4

Bo Heinemann, Jesper Morten Nielsen, Heidi Rye Hudlebusch, Michael J. Lees, Dorthe Vang Larsen, Thomas Boesen, Marc Labelle, Lars-Ole Gerlach, Peter Birk and Kristian Helin ()
Additional contact information
Bo Heinemann: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Jesper Morten Nielsen: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Heidi Rye Hudlebusch: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Michael J. Lees: Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen, Denmark
Dorthe Vang Larsen: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Thomas Boesen: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Marc Labelle: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Lars-Ole Gerlach: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Peter Birk: EpiTherapeutics Aps, Ole Maaløes Vej 3, 2200 Copenhagen, Denmark
Kristian Helin: Biotech Research and Innovation Centre (BRIC), University of Copenhagen, Ole Maaløes Vej 5, 2200 Copenhagen, Denmark

Nature, 2014, vol. 514, issue 7520, E1-E2

Abstract: Abstract Arising from L. Kruidenier et al. Nature 488, 404–408 (2012); doi:10.1038/nature11262 The recent publication1 of the first highly potent and specific inhibitor GSK-J1/J4 of the H3K27me3/me2-demethylases JMJD3/KDM6B and UTX/KDM6A provides a potential tool compound for this histone demethylase subfamily1. This inhibitor was used in tissue culture assays to conclude that the catalytic activities of the KDM6 proteins are required in inflammatory responses1; the generation of the inhibitor is intriguing, because it provides a strategy for generating sub-type-specific inhibitors of the 27-member Jumonji family and for the future treatment of various types of disease2,3,4,5,6. Here we show that the inhibitor is not specific for the H3K27me3/me2-demethylase subfamily in vitro and in tissue culture assays. Thus, the inhibitor cannot be used alone for drawing conclusions regarding the specific role of H3K27me3/me2-demethylase activity in biological processes or disease. There is a Reply to this Brief Communications Arising by Kruidenier et al. Nature 514, http://dx.doi.org/10.1038/nature13689 (2014).

Date: 2014
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DOI: 10.1038/nature13688

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