JAK2 phosphorylates histone H3Y41 and excludes HP1α from chromatin

Mark A. Dawson, Andrew J. Bannister, Berthold Göttgens, Samuel D. Foster, Till Bartke, Anthony R. Green () and Tony Kouzarides ()
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Mark A. Dawson: University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
Andrew J. Bannister: University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK
Berthold Göttgens: University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
Samuel D. Foster: University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
Till Bartke: University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK
Anthony R. Green: University of Cambridge, Hills Road, Cambridge CB2 0XY, UK
Tony Kouzarides: University of Cambridge, Tennis Court Road, Cambridge CB2 1QN, UK

Nature, 2009, vol. 461, issue 7265, 819-822

Abstract: JAK2 kinase goes nuclear JAK2 is a non-receptor tyrosine kinase that regulates diverse cellular processes by inducing cytoplasmic signalling cascades. Dawson et al. now report a previously unknown nuclear function for JAK2. Tyrosine phosphorylation of histone H3 by JAK2 can lead to disruption of HP1 α binding to chromatin and changes in gene expression. This finding is of particular interest because JAK2 inhibitors are in clinical trials for the treatment of myeloid leukaemias in which JAK2 is dysregulated.

Date: 2009
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DOI: 10.1038/nature08448

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