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Biochim Biophys Acta. 2014 Aug;1839(8):711-8. doi: 10.1016/j.bbagrm.2014.04.013. Epub 2014 Apr 18.

Sensing core histone phosphorylation - a matter of perfect timing.

Author information

1
Department of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, Vienna, Austria.
2
Department of Medical Biochemistry, Max F. Perutz Laboratories, Medical University of Vienna, Vienna Biocenter, Vienna, Austria. Electronic address: christian.seiser@univie.ac.at.

Abstract

Systematic analysis of histone modifications has revealed a plethora of posttranslational modifications that mediate changes in chromatin structure and gene expression. Histone phosphorylation is a transient histone modification that becomes induced by extracellular signals, DNA damage or entry into mitosis. Importantly, phosphorylation of histone proteins does lead not only to the binding of specific reader proteins but also to changes in the affinity for readers or writers of other histone modifications. This induces a cross-talk between different chromatin modifications that allows the spatio-temporal control of chromatin-associated events. In this review we will summarize the progress in our current knowledge of factors sensing reversible histone phosphorylation in different biological scenarios. This article is part of a Special Issue entitled: Molecular mechanisms of histone modification function.

KEYWORDS:

DNA damage; Histone code; Histone phosphorylation; Mitosis; Transcription

PMID:
24747175
PMCID:
PMC4103482
DOI:
10.1016/j.bbagrm.2014.04.013
[Indexed for MEDLINE]
Free PMC Article

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