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Cooperation of kindlin-3 and talin-1 in integrin activation during neutrophil arrest and inflammation

Wen, Lai1; Lee, Serena1

Published Feb 25, 2026 on Dryad. https://doi.org/10.5061/dryad.fttdz096g

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Abstract

Neutrophil arrest requires the activation of beta2 integrins. Two FERM domain proteins, kindlin-3 and talin-1, are necessary for neutrophil arrest. In this project, we explored the molecular mechanisms of talin-1 and kindlin-3 cooperation during neutrophil adhesion. Flow chamber experiments showed that talin-1 and kindlin-3 are simultaneously recruited to the plasma membrane of HL-60 cells during the transition from rolling to arrest. Using primary neutrophils expressing fluorescent fusion proteins of talin-1 or kindlin-3, we confirmed that both proteins are recruited to the plasma membrane at the time of arrest, supporting their coordinated role in neutrophil integrin activation. In a mouse cremaster muscle ischemia-reperfusion model, beta2 integrin activation was detected in neutrophils attached to the endothelium after ischemia-reperfusion. These findings support that kindlin-3 and talin-1 work together to induce high-affinity integrin activation during inflammation.