UFL1 promotes histone H4 ufmylation and ATM activation View Full Text


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2019-12

AUTHORS

Bo Qin, Jia Yu, Somaira Nowsheen, Minghui Wang, Xinyi Tu, Tongzheng Liu, Honglin Li, Liewei Wang, Zhenkun Lou

ABSTRACT

The ataxia-telangiectasia mutated (ATM) kinase, an upstream kinase of the DNA damage response (DDR), is rapidly activated following DNA damage, and phosphorylates its downstream targets to launch DDR signaling. However, the mechanism of ATM activation is still not completely understood. Here we report that UFM1 specific ligase 1 (UFL1), an ufmylation E3 ligase, is important for ATM activation. UFL1 is recruited to double strand breaks by the MRE11/RAD50/NBS1 complex, and monoufmylates histone H4 following DNA damage. Monoufmylated histone H4 is important for Suv39h1 and Tip60 recruitment. Furthermore, ATM phosphorylates UFL1 at serine 462, enhancing UFL1 E3 ligase activity and promoting ATM activation in a positive feedback loop. These findings reveal that ufmylation of histone H4 by UFL1 is an important step for amplification of ATM activation and maintenance of genomic integrity. More... »

PAGES

1242

References to SciGraph publications

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  • Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/s41467-019-09175-0

    DOI

    http://dx.doi.org/10.1038/s41467-019-09175-0

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1112856273

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/30886146


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