{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Xu J"],"funding":["NIAID NIH HHS"],"pagination":["eadl2993"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC12020992"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["10(103)"],"pubmed_abstract":["The NLRP3 inflammasome plays a critical role in innate immunity and inflammatory diseases. NIMA-related kinase 7 (NEK7) is essential for inflammasome activation, and its interaction with NLRP3 is enhanced by K<sup>+</sup> efflux. However, the mechanism by which K<sup>+</sup> efflux promotes this interaction remains unknown. Here, we show that NEK7 is rapidly phosphorylated at threonine-190/191 by JNK1 downstream of K<sup>+</sup> efflux and gasdermin D (GSDMD) after NLRP3 activation. NEK7 phosphorylation enhances the binding between NEK7 and NLRP3, which further promotes inflammasome assembly and activation. Mutant mice and macrophages in which Thr<sup>190</sup> and Thr<sup>191</sup> of Nek7 were replaced by valine exhibited impaired NEK7 phosphorylation, NLRP3 inflammasome activation, and "],"journal":["Science immunology"],"pubmed_title":["NEK7 phosphorylation amplifies NLRP3 inflammasome activation downstream of potassium efflux and gasdermin D."],"pmcid":["PMC12020992"],"funding_grant_id":["R01 AI148544","R37 AI063331"],"pubmed_authors":["He Y","Odeh N","Nunez G","Sun F","Zhang L","Xu J","Duan Y"],"additional_accession":[]},"is_claimable":false,"name":"NEK7 phosphorylation amplifies NLRP3 inflammasome activation downstream of potassium efflux and gasdermin D.","description":"The NLRP3 inflammasome plays a critical role in innate immunity and inflammatory diseases. NIMA-related kinase 7 (NEK7) is essential for inflammasome activation, and its interaction with NLRP3 is enhanced by K<sup>+</sup> efflux. However, the mechanism by which K<sup>+</sup> efflux promotes this interaction remains unknown. Here, we show that NEK7 is rapidly phosphorylated at threonine-190/191 by JNK1 downstream of K<sup>+</sup> efflux and gasdermin D (GSDMD) after NLRP3 activation. NEK7 phosphorylation enhances the binding between NEK7 and NLRP3, which further promotes inflammasome assembly and activation. Mutant mice and macrophages in which Thr<sup>190</sup> and Thr<sup>191</sup> of Nek7 were replaced by valine exhibited impaired NEK7 phosphorylation, NLRP3 inflammasome activation, and ","dates":{"release":"2025-01-01T00:00:00Z","publication":"2025 Jan","modification":"2026-06-06T19:35:52.078Z","creation":"2026-06-04T03:11:47.769Z"},"accession":"S-EPMC12020992","cross_references":{"pubmed":["39752537"],"doi":["10.1126/sciimmunol.adl2993"]}}