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

Shan Li, Li Zhang, Qing Yao, Lin Li, Na Dong, Jie Rong, Wenqing Gao, Xiaojun Ding, Liming Sun, Xing Chen, She Chen () and Feng Shao ()
Additional contact information
Shan Li: College of Biological Sciences, China Agricultural University
Li Zhang: National Institute of Biological Sciences
Qing Yao: College of Biological Sciences, China Agricultural University
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

Nature, 2013, vol. 501, issue 7466, 242-246

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.

Date: 2013
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature12436 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:501:y:2013:i:7466:d:10.1038_nature12436

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature12436

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().