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10.4049/jimmunol.1402951

http://scihub22266oqcxt.onion/10.4049/jimmunol.1402951
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C4340749!4340749!25637014
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suck abstract from ncbi


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pmid25637014      J+Immunol 2015 ; 194 (5): 2064-7
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  • SHANK-associated RH domain interacting protein (SHARPIN) is required for optimal NLRP3 inflammasome activation #MMPMID25637014
  • Gurung P; Lamkanfi M; Kanneganti TD
  • J Immunol 2015[Mar]; 194 (5): 2064-7 PMID25637014show ga
  • The NLRP3 inflammasome is a multimeric protein complex assembled in response to a wide array of pathogens and danger-associated molecular patterns. Despite the ability of NLRP3 to respond to diverse cues, the mechanisms controlling assembly of this complex are contested. Recently published studies show that HOIL-1, a member of the linear ubiquitin chain assembly complex (LUBAC), contributes to activation of the NLRP3 inflammasome. SHARPIN, along with HOIP and HOIL-1 assembles the LUBAC complex. Herein, we examined whether SHARPIN is required for the activation of NLRP3 inflammasome. Utilizing Sharpincpdm macrophages (deficient in SHARPIN expression), we demonstrate that SHARPIN is required for optimal activation of the NLRP3 inflammasome by both canonical and non-canonical stimuli. Furthermore, Sharpincpdm macrophages had dramatic defects in both NF?B and MAP kinase pathways, suggesting a role in transcriptional priming of the NLRP3 inflammasome. In conclusion, our study identified SHARPIN as a novel regulator of the NLRP3 inflammasome.
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