IndraLab

Statements

BRCC3 inhibits NLRP3. 4 / 4
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"Specifically, ox-LDL intensified the proteasomal and deubiquitinating activity of BRCC36, which decreased proteasomal degradation of the NLRP3 molecule and activated the NLRP3 inflammasome (Singh et al. 2019)."
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"Functionally, we show that lentivirus mediated overexpression of WWP2 in murine macrophages inhibits NLRP3 inflammasome activation by decreasing BRCC3 protein level."
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"Since BRCC3 is a DUB that mediates Lys48 deubiquitylation of NLRP3 (Py et al., 2013; Rao et al., 2019) degradation of BRCC3 induce NLRP3 downregulation (Zhang et al., 2022)."
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"BRCC3 knockdown leads to an increase in NLRP3 ubiquitination, and the DUB activity of BRCC3 is required for caspase-1 activation and IL-1beta processing, but not for LPS induced transcription of pro-IL-1beta or of NLRP3 itself XREF_BIBR."
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