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    A cytosolic Ezh1 isoform modulates a PRC2–Ezh1 epigenetic adaptive response in postmitotic cells

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    Type
    Article
    Authors
    Bodega, Beatrice
    Marasca, Federica
    Ranzani, Valeria
    Cherubini, Alessandro
    Valle, Francesco Della
    Neguembor, Maria Victoria
    Wassef, Michel
    Zippo, Alessio
    Lanzuolo, Chiara
    Pagani, Massimiliano
    Orlando, Valerio cc
    KAUST Department
    Biological and Environmental Sciences and Engineering (BESE) Division
    Bioscience Program
    Date
    2017-03-27
    Online Publication Date
    2017-03-27
    Print Publication Date
    2017-05
    Permanent link to this record
    http://hdl.handle.net/10754/623777
    
    Metadata
    Show full item record
    Abstract
    The evolution of chromatin-based epigenetic cell memory may be driven not only by the necessity for cells to stably maintain transcription programs, but also by the need to recognize signals and allow plastic responses to environmental stimuli. The mechanistic role of the epigenome in adult postmitotic tissues, however, remains largely unknown. In vertebrates, two variants of the Polycomb repressive complex (PRC2-Ezh2 and PRC2-Ezh1) control gene silencing via methylation of histone H3 on Lys27 (H3K27me). Here we describe a reversible mechanism that involves a novel isoform of Ezh1 (Ezh1β). Ezh1β lacks the catalytic SET domain and acts in the cytoplasm of skeletal muscle cells to control nuclear PRC2-Ezh1 activity in response to atrophic oxidative stress, by regulating Eed assembly with Suz12 and Ezh1α (the canonical isoform) at their target genes. We report a novel PRC2-Ezh1 function that utilizes Ezh1β as an adaptive stress sensor in the cytoplasm, thus allowing postmitotic cells to maintain tissue integrity in response to environmental changes.
    Citation
    Bodega B, Marasca F, Ranzani V, Cherubini A, Della Valle F, et al. (2017) A cytosolic Ezh1 isoform modulates a PRC2–Ezh1 epigenetic adaptive response in postmitotic cells. Nature Structural & Molecular Biology 24: 444–452. Available: http://dx.doi.org/10.1038/nsmb.3392.
    Sponsors
    We are grateful to C. Desplan, P. Sassone-Corsi, D. Gabellini, E. Battaglioli and S. Biffo for discussions and critical revision of the manuscript; G. Natoli (IFOM-IEO Campus, Milan, Italy) for sharing the Jmjd3 antibody; M. Mora (“Cells, tissues and DNA from patients with neuromuscular diseases” Telethon Biobank, Milan, Italy) for providing human primary myoblasts; R. Margueron (Institute Curie, Paris, France) for providing pCDNA-4TO-Ezh1α-HA plasmid; Sequentia Biotech SL, R. Bonnal and C. Cheroni for bioinformatical support; and M. Moro and M.C. Crosti for technical assistance with cell sorting. This work was supported by the EPIGEN Italian flagship program and King Abdullah University of Science and Technology (KAUST) (to V.O.).
    Publisher
    Springer Nature
    Journal
    Nature Structural & Molecular Biology
    DOI
    10.1038/nsmb.3392
    Additional Links
    http://www.nature.com/nsmb/journal/vaop/ncurrent/full/nsmb.3392.html
    ae974a485f413a2113503eed53cd6c53
    10.1038/nsmb.3392
    Scopus Count
    Collections
    Articles; Biological and Environmental Science and Engineering (BESE) Division; Bioscience Program

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