Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger

Gang G. Wang, Jikui Song, Zhanxin Wang, Holger L. Dormann, Fabio Casadio, Haitao Li, Jun-Li Luo, Dinshaw J. Patel and C. David Allis ()
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Gang G. Wang: Laboratory of Chromatin Biology & Epigenetics, The Rockefeller University, New York, New York 10065, USA
Jikui Song: Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA
Zhanxin Wang: Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA
Holger L. Dormann: Laboratory of Chromatin Biology & Epigenetics, The Rockefeller University, New York, New York 10065, USA
Fabio Casadio: Laboratory of Chromatin Biology & Epigenetics, The Rockefeller University, New York, New York 10065, USA
Haitao Li: Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA
Jun-Li Luo: The Scripps Research Institute, Scripps Florida, Jupiter, Florida 33458, USA
Dinshaw J. Patel: Structural Biology Program, Memorial Sloan-Kettering Cancer Center, New York, New York 10065, USA
C. David Allis: Laboratory of Chromatin Biology & Epigenetics, The Rockefeller University, New York, New York 10065, USA

Nature, 2009, vol. 459, issue 7248, 847-851

Abstract: Histones and leukaemia A chromosomal translocation found in certain acute myeloid leukaemia (AML) patients results in fusion of the PHD finger of a chromatin-binding protein to a nucleoporin NUP98. One such fusion protein is now reported to be a potent oncoprotein inducing AML. Introducing mutations in the PHD finger that abrogate its binding to histone H3 trimethylated at Lys4 is shown to abolish tumorigenesis. By binding chromatin, the NUP98-PHD fusion seems to lock developmentally important genes into an active state. Deregulation of an 'effector' of histone modifications can therefore lead to oncogenesis.

Date: 2009
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DOI: 10.1038/nature08036

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