G Protein Signaling Modulator-3 Inhibits the Inflammasome Activity of NLRP3

Patrick M. Giguère, Bryan J. Gall, Ejiofor A. D. Ezekwe, Geneviève Laroche, Brian K. Buckley, Chahnaz Kebaier, Justin E. Wilson, Jenny P. Ting, David P. Siderovski, Joseph A. Duncan
<span title="2014-09-30">2014</span> <i title="American Society for Biochemistry &amp; Molecular Biology (ASBMB)"> <a target="_blank" rel="noopener" href="https://fatcat.wiki/container/mryncoafc5cxdicldzfm4vlsze" style="color: black;">Journal of Biological Chemistry</a> </i> &nbsp;
NLRP3 is a key regulator of innate inflammation and is linked to inflammatory diseases. Results: GPSM3 associates with NLRP3 and inhibits its function. Conclusion: GPSM3 specifically inhibits NLRP3-dependent inflammasome activity by interacting with its leucine-rich repeat domain. Significance: This association uncovers a putative new mechanism of NLRP3 control, linking a G protein modulator to NLRP3-dependent inflammatory diseases.
<span class="external-identifiers"> <a target="_blank" rel="external noopener noreferrer" href="https://doi.org/10.1074/jbc.m114.578393">doi:10.1074/jbc.m114.578393</a> <a target="_blank" rel="external noopener" href="https://www.ncbi.nlm.nih.gov/pubmed/25271165">pmid:25271165</a> <a target="_blank" rel="external noopener" href="https://pubmed.ncbi.nlm.nih.gov/PMC4246083/">pmcid:PMC4246083</a> <a target="_blank" rel="external noopener" href="https://fatcat.wiki/release/tmolaq4m2fbszh3et22mkj5lxq">fatcat:tmolaq4m2fbszh3et22mkj5lxq</a> </span>
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