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Here, we describe two different classes of helical ESCRT-III filaments that can surround and tubulate membranes containing PIP\n                    <jats:sub>2<\/jats:sub>\n                    lipids. Cryo-EM reconstructions revealed that protofilaments comprising closed IST1 subunits formed 8-stranded nanotubes that encase membrane monolayers. The nanotube coordinates exposed PI(4,5)P\n                    <jats:sub>2<\/jats:sub>\n                    or PI(3,5)P\n                    <jats:sub>2<\/jats:sub>\n                    headgroups within a basic pocket formed at the junction of three IST1 subunits, and our structures reveal how the pocket can accommodate either PIP\n                    <jats:sub>2<\/jats:sub>\n                    isomer with minimal adjustment. In contrast, protofilaments comprising open CHMP1A subunits formed one start helices that encase membrane bilayers and bind exposed PI(4,5)P\n                    <jats:sub>2<\/jats:sub>\n                    headgroups across a basic surface that spans adjacent subunits of the CHMP1A protofilament. These two different structures extend the known plasticity of ESCRT-III polymers, reveal how PIP\n                    <jats:sub>2<\/jats:sub>\n                    lipids can promote ESCRT-III filament assembly and membrane remodeling, and define the molecular contacts that underlie specific ESCRT-III\/PIP\n                    <jats:sub>2<\/jats:sub>\n                    interactions.\n                  <\/jats:p>","DOI":"10.1073\/pnas.2616668123","type":"journal-article","created":{"date-parts":[[2026,6,30]],"date-time":"2026-06-30T17:43:55Z","timestamp":1782841435000},"update-policy":"https:\/\/doi.org\/10.1073\/pnas.cm10313","source":"Crossref","is-referenced-by-count":0,"title":["Phosphatidylinositol diphosphate binding by ESCRT-III filaments"],"prefix":"10.1073","volume":"123","author":[{"given":"Akram","family":"Alian","sequence":"first","affiliation":[{"id":[{"id":"https:\/\/ror.org\/03r0ha626","id-type":"ROR","asserted-by":"publisher"}],"name":"Department of Biochemistry, 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