Deubiquitination of NLRP3 by BRCC3 critically regulates inflammasome activity.

By B. Py, Mi-Sung Kim, H. Vakifahmetoglu-Norberg, Junying Yuan. Molecules and Cells, 2013

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Regulation of inflammasome activation (2015, background): “enzyme, leads to activation of the inflammasome (76, 77).”
NF-κB signaling in inflammation (2017, positive): “62, 63 Typical inducers of signal 1 include microbial components, such as TLR ligands, and cytokines like TNF-α and IL-1 β , which are known to activate NF-κ B, a transcriptional activator of both NLRP3 and pro-IL-1 β genes.”
Redox Regulation of NLRP3 Inflammasomes: ROS as Trigger or Effector? (2015, neutral): “Breast cancer 1 or 2 protein (BRCA1/BRCA2)-containing complex subunit 3, BRCC3 is an NLRP3-specific deubiquitinase enzyme that has recently been identified as the critical regulator of NLRP3 ubiquitination and its subsequent activation (110).”
Bile Acids Control Inflammation and Metabolic Disorder through Inhibition of NLRP3 Inflammasome. (2016, background): “Bile Acids and TGR5 Signaling Promote NLRP3 Ubiquitination Recent studies have shown that the deubiquitination of NLRP3 is critically involved in NLRP3 inflammasome activation, whereas inhibition of NLRP3 deubiquitination blocks both mouse and human NLRP3 activation (Juliana et al., 2012; Py et al.,”
Mechanism and regulation of NLRP3 inflammasome activation (2016, background): “Lys-63-specific deubiquitinase BRCC36 (BRCC3), a JAMM domain-containing Zn metalloprotease, promotes NLRP3 deubiquitination during priming and regulates NLRP3 activation [26].”