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J Immunol. 2019 Jan 1;202(1):218-227. doi: 10.4049/jimmunol.1800334. Epub 2018 Dec 3.

NLRP10 Affects the Stability of Abin-1 To Control Inflammatory Responses.

Author information

1
Institute of Nutritional Medicine, University of Hohenheim, 70593 Stuttgart, Germany; and.
2
Institute for Medical Microbiology, Immunology and Hygiene, University of Cologne, 50931 Cologne, Germany.
3
Institute of Nutritional Medicine, University of Hohenheim, 70593 Stuttgart, Germany; and Thomas.kufer@uni-hohenheim.de.

Abstract

NOD-like receptors (NLR) are critical regulators of innate immune signaling. The NLR family consists of 22 human proteins with a conserved structure containing a central oligomerization NACHT domain, an N-terminal interaction domain, and a variable number of C-terminal leucine-rich repeats. Most NLR proteins function as cytosolic pattern recognition receptors with activation of downstream inflammasome signaling, NF-κB, or MAPK activation. Although NLRP10 is the only NLR protein lacking the leucine rich repeats, it has been implicated in multiple immune pathways, including the regulation of inflammatory responses toward Leishmania major and Shigella flexneri infection. In this study, we identify Abin-1, a negative regulator of NF-κB, as an interaction partner of NLRP10 that binds to the NACHT domain of NLRP10. Using S. flexneri as an infection model in human epithelial cells, our work reveals a novel function of NLRP10 in destabilizing Abin-1, resulting in enhanced proinflammatory signaling. Our data give insight into the molecular mechanism underlying the function of NLRP10 in innate immune responses.

PMID:
30510071
DOI:
10.4049/jimmunol.1800334

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