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• W2904176489 abstract "Abstract Mutations in the nucleotide-binding oligomerization domain protein 12 (NLRP12) cause recurrent episodes of serosal inflammation. Here we show that NLRP12 efficiently sequesters HSP90 and promotes K48-linked ubiquitination and degradation of NOD2 in response to bacterial muramyl dipeptide (MDP). This interaction is mediated by the linker-region proximal to the nucleotide-binding domain of NLRP12. Consequently, the disease-causing NLRP12 R284X mutation fails to repress MDP-induced NF-κB and subsequent activity of the JAK/STAT signaling pathway. While NLRP12 deficiency renders septic mice highly susceptible towards MDP, a sustained sensing of MDP through NOD2 is observed among monocytes lacking NLRP12. This loss of tolerance in monocytes results in greater colonization resistance towards Citrobacter rodentium . Our data show that this is a consequence of NOD2-dependent accumulation of inflammatory mononuclear cells that correlates with induction of interferon-stimulated genes. Our study unveils a relevant process of tolerance towards the gut microbiota that is exploited by an attaching/effacing enteric pathogen." @default.
• W2904176489 created "2018-12-22" @default.
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• W2904176489 date "2018-12-17" @default.
• W2904176489 modified "2023-10-14" @default.
• W2904176489 title "Proteasomal degradation of NOD2 by NLRP12 in monocytes promotes bacterial tolerance and colonization by enteropathogens" @default.
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• W2904176489 doi "https://doi.org/10.1038/s41467-018-07750-5" @default.
• W2904176489 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6297353" @default.
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• W2904176489 hasPublicationYear "2018" @default.
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