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However, the precise mechanism of its release from the cytosolic compartment of neutrophils is unclear. Here, we show that E-selectin-induced rapid S100A8\/S100A9 release during inflammation occurs in an NLRP3 inflammasome-dependent fashion. Mechanistically, E-selectin engagement triggers Bruton\u2019s tyrosine kinase-dependent tyrosine phosphorylation of NLRP3. Concomitant potassium efflux via the voltage-gated potassium channel K\n                    <jats:sub>V<\/jats:sub>\n                    1.3 mediates ASC oligomerization. This is followed by caspase 1 cleavage and downstream activation of pore-forming gasdermin D, enabling cytosolic release of S100A8\/S100A9. Strikingly, E-selectin-mediated gasdermin D pore formation does not result in cell death but is a transient process involving activation of the ESCRT III membrane repair machinery. These data clarify molecular mechanisms of controlled S100A8\/S100A9 release from neutrophils and identify the NLRP3\/gasdermin D axis as a rapid and reversible activation system in neutrophils during inflammation.\n                  <\/jats:p>","DOI":"10.1038\/s41590-023-01656-1","type":"journal-article","created":{"date-parts":[[2023,10,30]],"date-time":"2023-10-30T13:02:06Z","timestamp":1698670926000},"page":"2021-2031","update-policy":"https:\/\/doi.org\/10.1007\/springer_crossmark_policy","source":"Crossref","is-referenced-by-count":105,"title":["E-selectin-mediated rapid NLRP3 inflammasome activation regulates S100A8\/S100A9 release from neutrophils via transient gasdermin D pore 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