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However, the recruitment of caspase-1 into the ASC speck for activation remains unclear. Here, we identified the ATPase Vps4B as a central component of the inflammasome that endogenously interacts with ASC and caspase-1, contributing to the activation of NLRP3 and AIM2 inflammasomes. Mechanistically, the polymerization of NLRP3 and ASC triggers intracellular Ca2+ signaling, which recruits Vps4B to the ASC speck. Vps4B forms a ring-like structure encircling the ASC filament and catalyzes the disassembly and liberation of the used caspase-1 CARD domain. This process enables replenishment and renewal of the newly unoccupied ASC speck, facilitating continuous caspase-1 recruitment and activation, thereby contributing to host defense against Listeria dissemination and the maintenance of blood\u2013brain barrier integrity in vivo. Our study identifies a self-rejuvenating inflammasome process that opens up new avenues for therapeutic intervention in inflammatory diseases.<\/jats:p>","DOI":"10.1084\/jem.20260373","type":"journal-article","created":{"date-parts":[[2026,7,11]],"date-time":"2026-07-11T06:20:52Z","timestamp":1783750852000},"update-policy":"https:\/\/doi.org\/10.1084\/jem.crossmarkpolicy","source":"Crossref","is-referenced-by-count":0,"title":["Vps4B controls caspase-1 dynamics at the ASC speck to drive inflammasome activation"],"prefix":"10.1084","volume":"223","author":[{"ORCID":"https:\/\/orcid.org\/0009-0006-4255-2657","authenticated-orcid":true,"given":"Yanfeng","family":"Li","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/0207yh398","id-type":"ROR","asserted-by":"publisher"}],"name":"Key Laboratory for Experimental Teratology of the Ministry of Education, Advanced Medical Research Institute, Qilu Hospital, Cheeloo College of Medicine, Shandong University 1 , 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