{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,5,21]],"date-time":"2026-05-21T06:29:00Z","timestamp":1779344940904,"version":"3.51.4"},"reference-count":73,"publisher":"Rockefeller University Press","issue":"3","content-domain":{"domain":["rupress.org"],"crossmark-restriction":true},"short-container-title":[],"published-print":{"date-parts":[[2000,8,7]]},"abstract":"<jats:p>Focal adhesions are an elaborate network of interconnecting proteins linking actin stress fibers to the extracellular matrix substrate. Modulation of the focal adhesion plaque provides a mechanism for the regulation of cellular adhesive strength. Using interference reflection microscopy, we found that activation of phosphoinositide 3-kinase (PI 3-kinase) by PDGF induces the dissipation of focal adhesions. Loss of this close apposition between the cell membrane and the extracellular matrix coincided with a redistribution of \u03b1-actinin and vinculin from the focal adhesion complex to the Triton X-100\u2013soluble fraction. In contrast, talin and paxillin remained localized to focal adhesions, suggesting that activation of PI 3-kinase induced a restructuring of the plaque rather than complete dispersion. Furthermore, phosphatidylinositol (3,4,5)-trisphosphate (PtdIns (3,4,5)-P3), a lipid product of PI 3-kinase, was sufficient to induce restructuring of the focal adhesion plaque. We also found that PtdIns (3,4,5)-P3 binds to \u03b1-actinin in PDGF-treated cells. Further evidence demonstrated that activation of PI 3-kinase by PDGF induced a decrease in the association of \u03b1-actinin with the integrin \u03b2 subunit, and that PtdIns (3,4,5)-P3 could disrupt this interaction in vitro. Modification of focal adhesion structure by PI 3-kinase and its lipid product, PtdIns (3,4,5)-P3, has important implications for the regulation of cellular adhesive strength and motility.<\/jats:p>","DOI":"10.1083\/jcb.150.3.627","type":"journal-article","created":{"date-parts":[[2002,7,26]],"date-time":"2002-07-26T16:45:41Z","timestamp":1027701941000},"page":"627-642","update-policy":"https:\/\/doi.org\/10.1083\/jcb.crossmarkpolicy","source":"Crossref","is-referenced-by-count":110,"title":["Restructuring of Focal Adhesion Plaques by Pi 3-Kinase"],"prefix":"10.1083","volume":"150","author":[{"given":"Jeffrey A.","family":"Greenwood","sequence":"first","affiliation":[{"name":"aDepartment of Pathology, Division of Molecular and Cellular Pathology,"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Anne B.","family":"Theibert","sequence":"additional","affiliation":[{"name":"bDepartment of Neurobiology, University of Alabama at Birmingham, Birmingham, Alabama 35294"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Glenn D.","family":"Prestwich","sequence":"additional","affiliation":[{"name":"cDepartment of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112"}],"role":[{"role":"author","vocabulary":"crossref"}]},{"given":"Joanne E.","family":"Murphy-Ullrich","sequence":"additional","affiliation":[{"name":"aDepartment of Pathology, Division of Molecular and Cellular Pathology,"}],"role":[{"role":"author","vocabulary":"crossref"}]}],"member":"291","published-online":{"date-parts":[[2000,8,7]]},"reference":[{"key":"2023072902223409400_Bladeretal1999","doi-asserted-by":"crossref","first-page":"581","DOI":"10.1091\/mbc.10.3.581","article-title":"GCS1, an arf guanosine triphosphate-activating protein in Saccharomyces cerevisiae, is required for normal actin cytoskeletal organization in vivo and stimulates actin polymerization in vitro","volume":"10","author":"Blader","year":"1999","journal-title":"Mol. 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