As part of the cytosolic BRISC complex (Cooper et al. 2009), BRCC3 regulates NLRP3 activity by promoting K63-deubiquitination of its LRR domain (Py et al. 2013). FAM175B (ABRO1), another BRISC subunit, binds directly to NLRP3 leading to FAM175B-dependent recruitment of the BRISC complex which mediates deubiquitination of NLRP3 upon inflammasome activation (Ren G et al.2019). In addition, FAM175B (ABRO1) enhanced BRCC3 protein stability by inhibiting WWP2-mediated ubiquitination and degradation of BRCC3 through the ubiquitin-proteasome pathway (Zhang W et al. 2021).The consequent activation of NLRP3 has been proposed to mediate necrotic cell sensing and the subsequent release of the proinflammatory cytokine IL-1Beta after hypoxic injury (Iyer et al. 2009).