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Despite increasing evidence of the proinflammatory effects of extracellular S100A8\/A9, little is known about its intracellular function. Here, we show that cytosolic S100A8\/A9 is indispensable for neutrophil post-arrest modifications during outside-in signaling under flow conditions in vitro and neutrophil recruitment in vivo, independent of its extracellular functions. Mechanistically, genetic deletion of S100A9 in mice caused dysregulated Ca\n                    <jats:sup>2+<\/jats:sup>\n                    signatures in activated neutrophils resulting in reduced Ca\n                    <jats:sup>2+<\/jats:sup>\n                    availability at the formed LFA-1\/F-actin clusters with defective \u03b2\n                    <jats:sub>2<\/jats:sub>\n                    integrin outside-in signaling during post-arrest modifications. Consequently, we observed impaired cytoskeletal rearrangement, cell polarization, and spreading, as well as cell protrusion formation in\n                    <jats:italic>\n                      S100a9\n                      <jats:sup>-\/-<\/jats:sup>\n                    <\/jats:italic>\n                    compared to wildtype (WT) neutrophils, making\n                    <jats:italic>\n                      S100a9\n                      <jats:sup>-\/-<\/jats:sup>\n                    <\/jats:italic>\n                    cells more susceptible to detach under flow, thereby preventing efficient neutrophil recruitment and extravasation into inflamed tissue.\n                  <\/jats:p>","DOI":"10.7554\/elife.96810","type":"journal-article","created":{"date-parts":[[2024,6,19]],"date-time":"2024-06-19T11:27:56Z","timestamp":1718796476000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.96810","source":"Crossref","is-referenced-by-count":2,"title":["Cytosolic S100A8\/A9 promotes Ca2+ 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