NLRP10 Affects the Stability of Abin-1 To Control Inflammatory Responses
Autor: | Katja Lautz, Thomas A. Kufer, Nora Mirza, Anna Sergeevna Sowa |
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Rok vydání: | 2019 |
Předmět: |
Inflammasomes
NLRP10 Immunology Leucine-rich repeat Shigella flexneri NLR Proteins Mice 03 medical and health sciences 0302 clinical medicine medicine Animals Humans Immunology and Allergy Adaptor Proteins Signal Transducing Dysentery Bacillary Inflammation Mice Knockout Innate immune system biology Protein Stability NF-kappa B Pattern recognition receptor Epithelial Cells Inflammasome biology.organism_classification Immunity Innate Cell biology DNA-Binding Proteins HEK293 Cells NACHT domain Apoptosis Regulatory Proteins Protein Binding Signal Transduction 030215 immunology medicine.drug |
Zdroj: | The Journal of Immunology. 202:218-227 |
ISSN: | 1550-6606 0022-1767 |
Popis: | 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. |
Databáze: | OpenAIRE |
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