{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,4,10]],"date-time":"2026-04-10T17:56:11Z","timestamp":1775843771772,"version":"3.50.1"},"reference-count":45,"publisher":"Wiley","issue":"2","license":[{"start":{"date-parts":[[2018,11,4]],"date-time":"2018-11-04T00:00:00Z","timestamp":1541289600000},"content-version":"vor","delay-in-days":0,"URL":"http:\/\/onlinelibrary.wiley.com\/termsAndConditions#vor"}],"funder":[{"DOI":"10.13039\/100000002","name":"National Institutes of Health","doi-asserted-by":"publisher","award":["DK28300"],"award-info":[{"award-number":["DK28300"]}],"id":[{"id":"10.13039\/100000002","id-type":"DOI","asserted-by":"publisher"}]}],"content-domain":{"domain":["onlinelibrary.wiley.com"],"crossmark-restriction":true},"short-container-title":["Neurogastroenterology Motil"],"published-print":{"date-parts":[[2019,2]]},"abstract":"<jats:title>Abstract<\/jats:title><jats:sec><jats:title>Background<\/jats:title><jats:p>Actin polymerization plays an important role in smooth muscle contraction. Integrin\u2010linked kinase (ILK) was shown to mediate actin polymerization in airway smooth muscle. The role of ILK in actin polymerization in response to m2 receptor activation was not in gastric smooth muscle.<\/jats:p><\/jats:sec><jats:sec><jats:title>Methods<\/jats:title><jats:p>Phosphorylation of paxillin, neuronal Wiskott\u2010Aldrich syndrome protein (N\u2010WASp), and association of paxillin with GEF proteins (Cool2\/\u03b1Pix [Cool2\/PAK\u2010interacting exchange factor alpha], Cool1\/\u03b2Pix [Cool1\/PAK\u2010interacting exchange factor beta], and DOCK 180 [Dedicator of cytokinesis]) and N\u2010WASp with Arp2\/3 complex were measured by western blot. Activation of Cdc42 was determined using an antibody for activated Cdc42. Actin polymerization was measured as an increase in F\u2010actin\/G\u2010actin ratio.<\/jats:p><\/jats:sec><jats:sec><jats:title>Results<\/jats:title><jats:p>Phosphorylation of paxillin, an association of paxillin with GEF proteins, Cdc42 activity, and actin polymerization were increased in response to m2 receptor activation in gastric smooth muscle cells. The increases in paxillin phosphorylation, Cdc42 activity, and actin polymerization were inhibited by a PI3K\u03b3 inhibitor (AS\u2010605240), ILK siRNA, and ILK dominant negative mutant (ILK [R211]). Increase in actin polymerization was also inhibited by Cdc42 dominant negative mutant (Cdc42 [T17N]). Increases in the association of paxillin with GEF proteins, phosphorylation of N\u2010WASp and its association with Arp2\/3 complex were inhibited by ILK (R211).<\/jats:p><\/jats:sec><jats:sec><jats:title>Conclusion<\/jats:title><jats:p>In gastric smooth muscle cells, activation of PI3K\u03b3 by muscarinic m2 receptors causes ILK\u2010dependent phosphorylation of paxillin, an association of paxillin with Cdc42 GEF proteins and activation of Cdc42, which, in turn, causes phosphorylation of N\u2010WASp and its association with Arp2\/3 complex leading to actin polymerization.<\/jats:p><\/jats:sec>","DOI":"10.1111\/nmo.13495","type":"journal-article","created":{"date-parts":[[2018,11,5]],"date-time":"2018-11-05T06:59:35Z","timestamp":1541401175000},"update-policy":"https:\/\/doi.org\/10.1002\/crossmark_policy","source":"Crossref","is-referenced-by-count":9,"title":["Muscarinic m2 receptor\u2010mediated actin polymerization via PI3 kinase \u03b3 and integrin\u2010linked kinase in gastric 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