When encountering membrane-associated antigen, mature follicular B-cells undergo rapid spreading, primarily driven by WASP-mediated branched actin polymerization, which maximizes B-cell contact with antigen-presenting surface and BCR-antigen engagement, amplifying signaling. Upon reaching maximal spreading, N-WASP distal to lamellipodial networks activates Arp2/3-mediated branched actin polymerization, which initiates the generation of inner F-actin foci from lamellipodia towards the center of the B-cell contact zone. NMII is then preferentially recruited to these relatively stable inner foci, which in turn promotes the centripetal movement of inner F-actin foci and the maturation of ring-like actomyosin structures, enabling B-cell contraction. B-cell contraction pushes the BCR microclusters formed during B-cell spreading to the center of the contact zone, increasing their molecular density. Increased molecular density promotes the disassociation of signaling molecules from BCR clusters, probably due to crowding and conformational changes, leading to signaling attenuation.