Activity-dependent phosphorylation of MeCP2 threonine 308 regulates interaction with NCoR

Daniel H. Ebert, Harrison W. Gabel, Nathaniel D. Robinson, Nathaniel R. Kastan, Linda S. Hu, Sonia Cohen, Adrija J. Navarro, Matthew J. Lyst, Robert Ekiert, Adrian P. Bird and Michael E. Greenberg ()
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Daniel H. Ebert: Harvard Medical School, Boston, Massachusetts 02115, USA
Harrison W. Gabel: Harvard Medical School, Boston, Massachusetts 02115, USA
Nathaniel D. Robinson: Harvard Medical School, Boston, Massachusetts 02115, USA
Nathaniel R. Kastan: Harvard Medical School, Boston, Massachusetts 02115, USA
Linda S. Hu: Harvard Medical School, Boston, Massachusetts 02115, USA
Sonia Cohen: Harvard Medical School, Boston, Massachusetts 02115, USA
Adrija J. Navarro: Harvard Medical School, Boston, Massachusetts 02115, USA
Matthew J. Lyst: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Robert Ekiert: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Adrian P. Bird: Wellcome Trust Centre for Cell Biology, University of Edinburgh
Michael E. Greenberg: Harvard Medical School, Boston, Massachusetts 02115, USA

Nature, 2013, vol. 499, issue 7458, 341-345

Abstract: Rett syndrome is caused by mutations in MeCP2, and this study identifies a site on MeCP2, T308, whose phosphorylation is regulated by neuronal activity: phosphorylation of T308 blocks the interaction of MeCP2 with the NCoR co-repressor complex, suppressing MeCP2's ability to repress transcription, and mice carrying mutations of MeCP2 T308 show Rett-syndrome-related symptoms.

Date: 2013
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DOI: 10.1038/nature12348

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