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Published, Version of Record (VoR)CC BY-NC V4.0, Open
Journal article
Modulation of H3.3 chromatin assembly by PML: A way to regulate epigenetic inheritance
BioEssays, v 43(10), 2100038
Oct 2021
PMID: 34423467
Featured in Collection : UN Sustainable Development Goals @ Drexel
Abstract
Although the promyelocytic leukemia (PML) protein is renowned for regulating a wide range of cellular processes and as an essential component of PML nuclear bodies (PML‐NBs), the mechanisms through which it exerts its broad physiological impact are far from fully elucidated. Here, we review recent studies supporting an emerging view that PML's pleiotropic effects derive, at least partially, from its role in regulating histone H3.3 chromatin assembly, a critical epigenetic mechanism. These studies suggest that PML maintains heterochromatin organization by restraining H3.3 incorporation. Examination of PML's contribution to H3.3 chromatin assembly in the context of the cell cycle and PML‐NB assembly suggests that PML represses heterochromatic H3.3 deposition during S phase and that transcription and SUMOylation regulate PML's recruitment to heterochromatin. Elucidating PML’ s contributions to H3.3‐mediated epigenetic regulation will provide insight into PML's expansive influence on cellular physiology and open new avenues for studying oncogenesis linked to PML malfunction.
Live cell and genomics analyses suggest that PML is recruited to DAXX and ATRX‐regulated heterochromatic loci during S phase to restrain H3.3 deposition. PML's function in H3.3 chromatin assembly is important for the epigenetic inheritance of transcriptional silencing through the maintenance of histone H3 lysine 9 trimethylation.
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Details
- Title
- Modulation of H3.3 chromatin assembly by PML: A way to regulate epigenetic inheritance
- Creators
- Erwan Delbarre - OsloMet – Oslo Metropolitan UniversitySusan M. Janicki - Drexel University Thomas R. Kline School of Law
- Publication Details
- BioEssays, v 43(10), 2100038
- Number of pages
- 13
- Grant note
- The Norwegian Cancer Society (6822903)
- Resource Type
- Journal article
- Language
- English
- Academic Unit
- Thomas R. Kline School of Law
- Web of Science ID
- WOS:000687105900001
- Scopus ID
- 2-s2.0-85113322186
- Other Identifier
- 991021860750704721
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- Collaboration types
- Domestic collaboration
- International collaboration
- Web of Science research areas
- Biochemistry & Molecular Biology
- Biology