Blood: Kindlin-3 mediats the molecular mechanisms activated by beta-2 integration.

The neutral granulocyte adhesion mediated by the integration begins with a rolling stop.
the activation of an integrator involves structural changes, from an inactive curved configuration to an extended image (E-plus) with high affinity for ligand binding (H-plus).
cytokine kindlin-3 is necessary for white blood cell adhesion;
the cytoploid tail of Kindlin-3 and beta-2 integrated proteins is different from that of Talin-1.
so far, the molecular mechanism by which Kindlin-3 activates beta-2 integrats is not fully clear.
the study, Wen and others measured the dynamic changes in the space-time composition of Kindlin-3 and beta-2 integratants in neutral granulocytes and HL-60 cells as they rolled and stagnated in a flowing state.
using a high-resolution dynamic footprint microscope and Kindlin-3-fluorescent protein (FP) fusion protein, the researchers found that Kindlin-3 was collected by IL-8 on the mass membrane before inducing changes in the composition of H-beta2.
(changes in adhesion of neogenic granulocytes on the endotkines of blood vessels before and after CXCL1 treatment) showed that neus granulocytes knocked out by the recombinant Kindlin-3 gene of EGFP-kindlin-3 stagnated in the body when stimulated by CXCL1.
EGFP-kindlin-3 in the neutral granulocytes of primary mice were also recruited into the mass membrane before stagnating.
, the researchers found small clusters of high-affinity Kindlin-2 integrative molecules over a large area of beta-3-FP near the membrane.
in neutral granulocyte HL-60 cells, the absence of Kindlin-3 or its Pleckstrin isotope gene (PH) completely abolishes the induction of H-beta-2 integration.
IL-8 can also trigger the collection of free Kindlin-3 PH domains on the mass membrane before stalling.
above, the study proves that the Kindlin-3 PH domain is essential for mass membrane recruitment, while the full-length Kindlin-3 is essential for inducing high affinity beta-2 integration.
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