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Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains

Author

Listed:
  • Shan Li

    (College of Biological Sciences, China Agricultural University
    National Institute of Biological Sciences)

  • Li Zhang

    (National Institute of Biological Sciences
    Graduate School of Chinese Academy of Medical Sciences and Beijing Union Medical College)

  • Qing Yao

    (College of Biological Sciences, China Agricultural University
    National Institute of Biological Sciences)

  • Lin Li

    (National Institute of Biological Sciences)

  • Na Dong

    (National Institute of Biological Sciences)

  • Jie Rong

    (Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University)

  • Wenqing Gao

    (National Institute of Biological Sciences)

  • Xiaojun Ding

    (National Institute of Biological Sciences)

  • Liming Sun

    (National Institute of Biological Sciences)

  • Xing Chen

    (Beijing National Laboratory for Molecular Sciences, College of Chemistry and Molecular Engineering, Peking University)

  • She Chen

    (National Institute of Biological Sciences)

  • Feng Shao

    (National Institute of Biological Sciences)

Abstract

Several death-domain-containing proteins are directly inactivated by the enteropathogenic Escherichia coli type III secretion system effector NleB; NleB functions as an N-acetylglucosamine transferase that modifies a conserved death domain arginine residue, blocking the receptor–adapter interaction.

Suggested Citation

  • Shan Li & Li Zhang & Qing Yao & Lin Li & Na Dong & Jie Rong & Wenqing Gao & Xiaojun Ding & Liming Sun & Xing Chen & She Chen & Feng Shao, 2013. "Pathogen blocks host death receptor signalling by arginine GlcNAcylation of death domains," Nature, Nature, vol. 501(7466), pages 242-246, September.
    • Handle: RePEc:nat:nature:v:501:y:2013:i:7466:d:10.1038_nature12436
    DOI: 10.1038/nature12436
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