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Aberrant activation of NLRP3 inflammasome is closely related to various inflammatory diseases. Post\u2010translational modifications are critical for NLRP3 inflammasome regulation. However, the mechanism of NLRP3 inflammasome activation remains incompletely understood. Here, it is demonstrated that the Ufm1 E3 ligase Ufl1 mediated UFMylation is essential for NLRP3 inflammasome activation. Mechanistically, Ufl1 binds and UFMylates NLRP3 in the priming stage of NLRP3 activation, thereby sustaining the stability of NLRP3 by preventing NLRP3 K63\u2010linked ubiquitination and the subsequent autophagic degradation. It is further demonstrated that myeloid cell\u2010specific\n                    <jats:italic>Ufl1<\/jats:italic>\n                    or\n                    <jats:italic>Ufm1<\/jats:italic>\n                    deficiency in mice significantly alleviated inflammatory responses and tissue damage following lipopolysaccharide (LPS)\u2010induced endotoxemia and alum\u2010induced peritonitis. Thus, the findings offer new insights into potential therapeutic targets for NLRP3 inflammasome\u2010related diseases by targeting the UFMylation system.\n                  <\/jats:p>","DOI":"10.1002\/advs.202406786","type":"journal-article","created":{"date-parts":[[2025,2,22]],"date-time":"2025-02-22T03:45:04Z","timestamp":1740195904000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":19,"title":["UFMylation of NLRP3 Prevents Its Autophagic Degradation and Facilitates Inflammasome Activation"],"prefix":"10.1002","volume":"12","author":[{"given":"Jiongjie","family":"Jing","sequence":"first","affiliation":[{"name":"State Key Laboratory of Cardiovascular Diseases and Medical Innovation Center Shanghai East Hospital School of Life Sciences and Technology Tongji University  Shanghai 200127 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