Phosphorylation of serine 10 in histone H3, what for?

Abstract : Eukaryotic cells must possess mechanisms for condensing and decondensing chromatin. Chromatin condensation is particularly evident during mitosis and cell death induced by apoptosis, whereas chromatin decondensation is necessary for replication, repair, recombination and transcription. Histones are among the numerous DNA-binding proteins that control the level of DNA condensation, and post-translational modification of histone tails plays a critical role in the dynamic condensation/decondensation that occurs during the cell cycle. Phosphorylation of Ser10 in the tails of histone H3 has been extensively studied in many organisms. Interestingly, this modification is involved in both transcription and cell division, two events requiring opposite alterations in the degree of chromatin compaction. How does one and the same modification of histone H3 fulfil such roles? For instance, in interphase, phosphorylation of H3 correlates with chromatin relaxation and gene expression, whereas in mitosis it correlates with chromosome condensation. What is the kinase and under what circumstances does Ser10 becomes phosphorylated? Most importantly, what are the consequences of phosphorylation of this residue?
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Journal of Cell Science, Company of Biologists, 2003, 116 (Pt 18), pp.3677-85. 〈10.1242/jcs.00735〉
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Contributeur : Claude Prigent <>
Soumis le : mercredi 26 mars 2014 - 16:57:17
Dernière modification le : mercredi 16 mai 2018 - 11:23:33

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Claude Prigent, Stefan Dimitrov. Phosphorylation of serine 10 in histone H3, what for?. Journal of Cell Science, Company of Biologists, 2003, 116 (Pt 18), pp.3677-85. 〈10.1242/jcs.00735〉. 〈inserm-00966495〉

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