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Details on Person In vitro binding assay showed that tripartite motif containi...
| Class:Id | Summation:9792886 |
|---|---|
| _displayName | In vitro binding assay showed that tripartite motif containi... |
| _timestamp | 2022-06-10 15:50:56 |
| created | [InstanceEdit:9792844] Shamovsky, Veronica, 2022-05-31 |
| literatureReference | [LiteratureReference:9792880] AKT Regulates NLRP3 Inflammasome Activation by Phosphorylating NLRP3 Serine 5 [LiteratureReference:9792853] TRIM31 inhibits NLRP3 inflammasome and pyroptosis of retinal pigment epithelial cells through ubiquitination of NLRP3 [LiteratureReference:9792839] The E3 ubiquitin ligase TRIM31 attenuates NLRP3 inflammasome activation by promoting proteasomal degradation of NLRP3 [LiteratureReference:9793336] Sequential ubiquitination of NLRP3 by RNF125 and Cbl-b limits inflammasome activation and endotoxemia |
| modified | [InstanceEdit:9793123] Shamovsky, Veronica, 2022-06-03 [InstanceEdit:9793333] Shamovsky, Veronica, 2022-06-10 |
| text | In vitro binding assay showed that tripartite motif containing protein 31 (TRIM31) directly binds to NLRP3 (Song H et al. 2016). Co-immunoprecipitation assay detected association between endogenous TRIM31 and NLRP3 in mouse peritoneal macrophages and human leukemia monocytic THP-1 cells (Song H et al. 2016). Further, overexpressed TRIM31 interacted with NLRP3 in human retinal pigment epithelial ARPE-19 cells (Huang P et al. 2020). The binding between TRIM31 and NLRP3 was also detected in human embryonic kidney HEK293T cells upon co-expression of tagged proteins (Song H et al. 2016). Colocalization assay using HEK293T cells further confirmed the interaction between TRIM31 and NLRP3. Mutagenesis assay showed that the C-terminal coiled-coil domain of TRIM31 and the PYD domain of NLRP3 are required for the NLRP3:TRIM31 interaction (Song H et al. 2016). These data suggest that NLRP3 directly interacts with TRIM31. However, no interaction between NLRP3 and TRIM31 was detected by glutathione-S-Transferase (GST) coupled with LC-MS/MS analysis in mouse bone marrow-derived macrophages (BMDM) (Tang J et al. 2020). The E3 ubiquitin ligase activity of TRIM31 was found to downregulate the inflammasome activation through promoting K48-linked polyubiquitination and proteasomal degradation of NLRP3 (Song H et al. 2016; Zhao W et al. 2020; Huang P et al. 2020). This Reactome event describes binding between NLRP3 and TRIM31. |
| (summation) | [Reaction:9792869] NLRP3 binds TRIM31 [Homo sapiens] |
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