IndraLab

Statements


5 | 14

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"To investigate the expression of BRCC3 and the interaction between NLRP3 and BRCC3 in H/R-induced pyroptosis and cell damage, BRCC3 expression was depleted by the transfection of BRCC3-shRNA into cells prior to induction of hypoxia (Fig. 2A)."

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"Aberrant ubiquitination of NLRP3 in ABRAXAS2-deficient cells appears to limit interactions between NLRP3 and ASC, rather than target NLRP3 for degradation.Biochemical experiments suggest that ABRAXAS2 and BRCC3 associate with NLRP3 after priming."

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"We therefore examined whether NLRP3 phosphorylation regulates the interaction between BRCC3 and NLRP3."

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"The association between ABRAXAS2 and BRCC3 and NLRP3 depends on the phosphorylation of NLRP3 serine 194 and the NLRP3 interactor NIMA-related kinase 7 (NEK7), which acts as a scaffold for bridging adjacent NLRP3 subunits and requires proposed priming [124,125]."

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"BRCC3 binds directly to NLRP3 and promotes the NLRP3 inflammasome activation through its deubiquitination [13]."

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"Co-IP experiments confirmed the interaction between BRCC3 and NLRP3."

No evidence text available

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"18 BRCC3 can directly bind to NLRP3 and favors NLRP3 inflammasome activation through its deubiquitination."

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"Furthermore, NLRP3 needs to be dephosphorylated at S806 to interact with and be deubiquitinated by BRCC3, and interaction of NLRP3 with NEK7 is required for subsequent BRCC3 recruitment and deubiquitylation of NLRP3 (49)."

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"To verify that NLRP3-BRCC3 complex formation is increased by cholesterol accumulation, we pulled down endogenous BRCC3 in acLDL-loaded BMDMs."

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"These findings suggest that increased NLRP3 deubiquitylation mediated through BRCC3/NLRP3 complex formation is a key mechanism underlying NLRP3 inflammasome activation in response to macrophage cholesterol loading.Recently, we showed that JNK was activated due to the decreased Dual-specificity phosphatase 10 (Dusp10) expression in Tet methylcytosine dioxygenase 2 (TET2) deficient macrophages (42)."

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"BRCC3 can directly bind to NLRP3 and favors NLRP3 inflammasome activation through its deubiquitination."
| PMC

No evidence text available

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"Another study found that VDR interferes with NLRP3 activation by disrupting deubiquitinase BRCC3-NLRP3 complex to promote NLRP3 degradation in bone marrow-derived macrophage [49]."

No evidence text available

No evidence text available

No evidence text available

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"This work suggested that BRCC3 directly interacted with NLRP3, and its presence was required for appropriate NLRP3 inflammasome formation."

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"VDR can bind to NLRP3 and prevent the process of deubiquitination (NLRP3 activation) mediated by the interaction between NLRP3 and BRCC3 [118]."