{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,9,20]],"date-time":"2026-09-20T03:57:43Z","timestamp":1789876663629,"version":"4.0.1"},"reference-count":28,"publisher":"National Academy of Sciences","issue":"18","content-domain":{"domain":["www.pnas.org"],"crossmark-restriction":true},"short-container-title":["Proc. Natl. Acad. Sci. U.S.A."],"published-print":{"date-parts":[[2013,4,30]]},"abstract":"<jats:p>\n                    The membrane\u2013cytosol interface is the major locus of control of actin polymerization. At this interface, phosphoinositides act as second messengers to recruit membrane-binding proteins. We show that curved membranes, but not flat ones, can use phosphatidylinositol 3-phosphate [PI(3)P] along with phosphatidylinositol 4,5-bisphosphate [PI(4,5)P\n                    <jats:sub>2<\/jats:sub>\n                    ] to stimulate actin polymerization. In this case, actin polymerization requires the small GTPase cell cycle division 42 (Cdc42), the nucleation-promoting factor neural Wiskott\u2013Aldrich syndrome protein (N-WASP) and the actin nucleator the actin-related protein (Arp) 2\/3 complex. In liposomes containing PI(4,5)P2 as the sole phosphoinositide, actin polymerization requires transducer of Cdc42 activation-1 (toca-1). In the presence of phosphatidylinositol 3-phosphate, polymerization is both more efficient and independent of toca-1. Under these conditions, sorting nexin 9 (Snx9) can be implicated as a specific adaptor that replaces toca-1 to mobilize neural Wiskott\u2013Aldrich syndrome protein and the Arp2\/3 complex. This switch in phosphoinositide and adaptor specificity for actin polymerization from membranes has implications for how different types of actin structures are generated at precise times and locations in the cell.\n                  <\/jats:p>","DOI":"10.1073\/pnas.1305286110","type":"journal-article","created":{"date-parts":[[2013,4,15]],"date-time":"2013-04-15T21:53:08Z","timestamp":1366062788000},"page":"7193-7198","update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":64,"title":["Phosphoinositides and membrane curvature switch the mode of actin polymerization via selective recruitment of toca-1 and Snx9"],"prefix":"10.1073","volume":"110","author":[{"given":"Jennifer L.","family":"Gallop","sequence":"first","affiliation":[{"name":"Department of Systems Biology, Harvard Medical School, Boston, MA 02115;"},{"name":"Wellcome Trust\/Cancer Research UK Gurdon Institute and Department of Biochemistry, University of Cambridge, Cambridge CB2 1QN, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Astrid","family":"Walrant","sequence":"additional","affiliation":[{"name":"Wellcome Trust\/Cancer Research UK Gurdon Institute and Department of Biochemistry, University of Cambridge, Cambridge CB2 1QN, United Kingdom; and"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Lewis C.","family":"Cantley","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Harvard Medical School, Boston, MA 02115;"},{"name":"Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, MA 02215"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Marc W.","family":"Kirschner","sequence":"additional","affiliation":[{"name":"Department of Systems Biology, Harvard Medical School, Boston, MA 02115;"}],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"341","published-online":{"date-parts":[[2013,4,15]]},"reference":[{"key":"e_1_3_3_1_2","doi-asserted-by":"publisher","DOI":"10.1083\/jcb.140.5.1125"},{"key":"e_1_3_3_2_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2004.11.054"},{"key":"e_1_3_3_3_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.molcel.2009.10.024"},{"key":"e_1_3_3_4_2","doi-asserted-by":"publisher","DOI":"10.1152\/physrev.00036.2009"},{"key":"e_1_3_3_5_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.bpj.2010.01.046"},{"key":"e_1_3_3_6_2","doi-asserted-by":"publisher","DOI":"10.1038\/nature04396"},{"key":"e_1_3_3_7_2","doi-asserted-by":"publisher","DOI":"10.1126\/science.1191710"},{"key":"e_1_3_3_8_2","doi-asserted-by":"publisher","DOI":"10.1016\/j.cell.2004.06.027"},{"key":"e_1_3_3_9_2","doi-asserted-by":"publisher","DOI":"10.1038\/emboj.2008.216"},{"key":"e_1_3_3_10_2","doi-asserted-by":"publisher","DOI":"10.1038\/ncb2094"},{"key":"e_1_3_3_11_2","doi-asserted-by":"publisher","DOI":"10.1371\/journal.pbio.1000604"},{"key":"e_1_3_3_12_2","doi-asserted-by":"crossref","unstructured":"S Hubner et al. 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