{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,23]],"date-time":"2026-10-23T03:18:17Z","timestamp":1792725497442,"version":"4.5.0"},"reference-count":65,"publisher":"American Society for Cell Biology (ASCB)","issue":"5","content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["MBoC"],"published-print":{"date-parts":[[2025,5,1]]},"abstract":"<jats:p>\n                    Sorting nexin 9 (SNX9) is a membrane-binding scaffold protein that contributes to viral uptake and inflammation and is associated with worse outcomes in several cancers. It is involved in endocytosis of epidermal growth factor receptors, \u03b21-integrin and membrane type 1 matrix metalloprotease, and formation of mitochondrial-derived vesicles. The SNX9 Bin-Amphiphysin-Rvs (BAR)-Phox homology (PX) domains bind phosphoinositide lipids and the Src homology 3 (SH3) domain interacts with dynamin and Neural-Wiskott Aldrich syndrome protein (N-WASP) to stimulate Arp2\/3 complex\u2013mediated actin polymerization. Here we use biolayer interferometry, cell-free reconstitution, and superresolution microscopy to analyze the specificity and activities of SNX9 at membranes. We find that more SNX9 can bind liposomes containing phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P\n                    <jats:sub>2<\/jats:sub>\n                    ) and phosphatidylinositol (3)-phosphate (PI(3)P) compared with phosphatidylinositol (3,4)-bisphosphate (PI(3,4)P\n                    <jats:sub>2<\/jats:sub>\n                    ), despite similar affinities. Actin assembly requires the network of both PX-BAR and SH3 interactions. Three-dimensional direct stochastic optical reconstruction microscopy on filopodia-like reconstitutions shows that SNX9 and related protein transducer of Cdc42-dependent actin assembly-1 (TOCA-1) can form both flat and \u223c0.5 \u00b5m curved assemblies at actin incorporation sites. Finally, using cryo-electron tomography, we show that SNX9 builds both branched and bundled actin networks demonstrating its potential for multifunctional roles in actin remodeling.\n                  <\/jats:p>","DOI":"10.1091\/mbc.e24-09-0419","type":"journal-article","created":{"date-parts":[[2025,3,19]],"date-time":"2025-03-19T12:11:23Z","timestamp":1742386283000},"source":"Crossref","is-referenced-by-count":2,"title":["Membrane composition and curvature in SNX9-mediated actin polymerization"],"prefix":"10.1091","volume":"36","author":[{"given":"Pankti","family":"Vaishnav","sequence":"first","affiliation":[{"name":"Gurdon Institute, University of Cambridge, Cambridge CB2 1QN, United Kingdom"},{"name":"Department of Biochemistry, University of Cambridge, Cambridge CB2 1GA, United Kingdom"}],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Hanae Shimo","family":"Kondo","sequence":"additional","affiliation":[{"name":"Gurdon Institute, University of Cambridge, Cambridge 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