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O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress

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  • Cuifang Han

    (Ocean University of China
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Yuchao Gu

    (Ocean University of China
    Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Hui Shan

    (Ocean University of China
    Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Wenyi Mi

    (Ocean University of China
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Jiahui Sun

    (Ocean University of China
    Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Minghui Shi

    (Ocean University of China
    Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Xinling Zhang

    (Ocean University of China
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Xinzhi Lu

    (Ocean University of China
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Feng Han

    (Ocean University of China
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Qianhong Gong

    (Ocean University of China
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

  • Wengong Yu

    (Ocean University of China
    Laboratory for Marine Drugs and Bioproducts of Qingdao National Laboratory for Marine Science and Technology
    Ministry of Education
    Key Laboratory of Glycoscience & Glycotechnology of Shandong Province)

Abstract

SIRT1 is the most evolutionarily conserved mammalian sirtuin, and it plays a vital role in the regulation of metabolism, stress responses, genome stability, and ageing. As a stress sensor, SIRT1 deacetylase activity is significantly increased during stresses, but the molecular mechanisms are not yet fully clear. Here, we show that SIRT1 is dynamically modified with O-GlcNAc at Ser 549 in its carboxy-terminal region, which directly increases its deacetylase activity both in vitro and in vivo. The O-GlcNAcylation of SIRT1 is elevated during genotoxic, oxidative, and metabolic stress stimuli in cellular and mouse models, thereby increasing SIRT1 deacetylase activity and protecting cells from stress-induced apoptosis. Our findings demonstrate a new mechanism for the activation of SIRT1 under stress conditions and suggest a novel potential therapeutic target for preventing age-related diseases and extending healthspan.

Suggested Citation

  • Cuifang Han & Yuchao Gu & Hui Shan & Wenyi Mi & Jiahui Sun & Minghui Shi & Xinling Zhang & Xinzhi Lu & Feng Han & Qianhong Gong & Wengong Yu, 2017. "O-GlcNAcylation of SIRT1 enhances its deacetylase activity and promotes cytoprotection under stress," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01654-6
    DOI: 10.1038/s41467-017-01654-6
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    Cited by:

    1. Leandro R. Soria & Georgios Makris & Alfonso M. D’Alessio & Angela Angelis & Iolanda Boffa & Veronica M. Pravata & Véronique Rüfenacht & Sergio Attanasio & Edoardo Nusco & Paola Arena & Andrew T. Fere, 2022. "O-GlcNAcylation enhances CPS1 catalytic efficiency for ammonia and promotes ureagenesis," Nature Communications, Nature, vol. 13(1), pages 1-14, December.

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