Post-Translational Modifications of H2A Histone Variants and Their Role in Cancer
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- David Corujo
- Josep Carreras Leukaemia Research Institute (IJC), Campus ICO-Germans Trias i Pujol, Universitat Autònoma de Barcelona, 08916 Badalona, Spain
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- Marcus Buschbeck
- Josep Carreras Leukaemia Research Institute (IJC), Campus ICO-Germans Trias i Pujol, Universitat Autònoma de Barcelona, 08916 Badalona, Spain
書誌事項
- 公開日
- 2018-02-27
- 権利情報
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- https://creativecommons.org/licenses/by/4.0/
- DOI
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- 10.3390/cancers10030059
- 公開者
- MDPI AG
説明
<jats:p>Histone variants are chromatin components that replace replication-coupled histones in a fraction of nucleosomes and confer particular characteristics to chromatin. H2A variants represent the most numerous and diverse group among histone protein families. In the nucleosomal structure, H2A-H2B dimers can be removed and exchanged more easily than the stable H3-H4 core. The unstructured N-terminal histone tails of all histones, but also the C-terminal tails of H2A histones protrude out of the compact structure of the nucleosome core. These accessible tails are the preferential target sites for a large number of post-translational modifications (PTMs). While some PTMs are shared between replication-coupled H2A and H2A variants, many modifications are limited to a specific histone variant. The present review focuses on the H2A variants H2A.Z, H2A.X, and macroH2A, and summarizes their functions in chromatin and how these are linked to cancer development and progression. H2A.Z primarily acts as an oncogene and macroH2A and H2A.X as tumour suppressors. We further focus on the regulation by PTMs, which helps to understand a degree of context dependency.</jats:p>
収録刊行物
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- Cancers
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Cancers 10 (3), 59-, 2018-02-27
MDPI AG
