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The actin cytoskeleton plays essential roles in BCR signaling. Upon encountering cell-surface antigens, actin-driven B-cell spreading amplifies signaling, while B-cell contraction following spreading leads to signal attenuation. However, the mechanism by which actin dynamics switch BCR signaling from amplification to attenuation is unknown. Here, we show that Arp2\/3-mediated branched actin polymerization is required for mouse splenic B-cell contraction. Contracting B-cells generate centripetally moving actin foci from lamellipodial F-actin networks in the plasma membrane region contacting antigen-presenting surfaces. Actin polymerization driven by N-WASP, but not WASP, initiates these actin foci and facilitates non-muscle myosin II recruitment to the contact zone, creating actomyosin ring-like structures. B-cell contraction increases BCR molecular density in individual clusters, leading to decreased BCR phosphorylation. Increased BCR molecular density reduced levels of the stimulatory kinase Syk, the inhibitory phosphatase SHIP-1, and their phosphorylated forms in individual BCR clusters. These results suggest that N-WASP-activated Arp2\/3, coordinating with myosin, generates centripetally moving foci and contractile actomyosin ring-like structures from lamellipodial networks, enabling contraction. B-cell contraction attenuates BCR signaling by pushing out both stimulatory kinases and inhibitory phosphatases from BCR clusters, providing novel insights into actin-facilitated signal attenuation.<\/jats:p>","DOI":"10.7554\/elife.87833","type":"journal-article","created":{"date-parts":[[2023,6,23]],"date-time":"2023-06-23T08:13:19Z","timestamp":1687507999000},"update-policy":"https:\/\/doi.org\/10.7554\/elife.87833","source":"Crossref","is-referenced-by-count":4,"title":["N-WASP-dependent branched actin polymerization attenuates B-cell receptor signaling by increasing the molecular density of receptor clusters"],"prefix":"10.7554","volume":"12","author":[{"given":"Anshuman","family":"Bhanja","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Cell Biology and Molecular Genetics, University of Maryland","place":["College Park, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Margaret K","family":"Seeley-Fallen","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Cell Biology and Molecular Genetics, University of Maryland","place":["College Park, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Michelle","family":"Lazzaro","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Cell Biology and Molecular Genetics, University of Maryland","place":["College Park, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Arpita","family":"Upadhyaya","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Biophysics Program, University of Maryland","place":["College Park, United States"]},{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Physics, University of Maryland","place":["College Park, United States"]},{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Institute for Physical Science and Technology, University of Maryland","place":["College Park, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]},{"ORCID":"https:\/\/orcid.org\/0000-0001-8795-8657","authenticated-orcid":true,"given":"Wenxia","family":"Song","sequence":"additional","affiliation":[{"id":[{"id":"https:\/\/ror.org\/047s2c258","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Cell Biology and Molecular Genetics, University of Maryland","place":["College Park, United States"]}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"4374","published-online":{"date-parts":[[2023,12,12]]},"reference":[{"key":"bib1","doi-asserted-by":"publisher","first-page":"26648","DOI":"10.1074\/jbc.M100997200","article-title":"SHP-1 requires inhibitory co-receptors to down-modulate B cell antigen receptor-mediated phosphorylation of cellular substrates","volume":"276","author":"Adachi","year":"2001","journal-title":"The Journal of Biological Chemistry"},{"key":"bib2","doi-asserted-by":"publisher","first-page":"33922","DOI":"10.1074\/jbc.273.51.33922","article-title":"The inositol phosphatase SHIP inhibits Akt\/PKB activation in B cells","volume":"273","author":"Aman","year":"1998","journal-title":"The Journal of Biological Chemistry"},{"key":"bib3","doi-asserted-by":"publisher","first-page":"15","DOI":"10.1038\/nri2454","article-title":"The who, how and where of antigen presentation to B cells","volume":"9","author":"Batista","year":"2009","journal-title":"Nature Reviews. 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