GlcNAcylation of a histone methyltransferase in retinoic-acid-induced granulopoiesis

Ryoji Fujiki, Toshihiro Chikanishi, Waka Hashiba, Hiroaki Ito, Ichiro Takada, Robert G. Roeder, Hirochika Kitagawa and Shigeaki Kato ()
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Ryoji Fujiki: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Toshihiro Chikanishi: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Waka Hashiba: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Hiroaki Ito: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Ichiro Takada: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Robert G. Roeder: Laboratory of Biochemistry and Molecular Biology, The Rockefeller University, 1230 York Avenue, New York, New York 10021, USA
Hirochika Kitagawa: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan
Shigeaki Kato: Institute of Molecular and Cellular Biosciences, University of Tokyo, 1-1-1 Yayoi, Bunkyo-ku, Tokyo 113-0032, Japan

Nature, 2009, vol. 459, issue 7245, 455-459

Abstract: GlcNAcylation of chromatin proteins in granulopoiesis The SET-domain-containing MLL proteins methylate histone H3 on lysine 4 and contribute to gene activation. Here, MLL5 is shown to associate in a complex with the retinoic acid receptor RARα and to be modified by O-linked β-N-acetylglucosamine (O-GlcNAc). Nuclear GlcNAcylation of MLL5 facilitates its activity as a co-activator of RARα target genes during granulopoiesis. This work points to an important role for GlcNAcylation in modifying chromatin proteins.

Date: 2009
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DOI: 10.1038/nature07954

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