Database of articles cited by EMDB/PDB/SASBDB data

Keywords
Structure methods	All X-ray diffraction NMR electron microscopy small angle scattering neutron diffraction fiber diffraction powder diffraction infrared spectroscopy EPR fluorescence transfer theoretical model Hybrid
Author
Journal
IF	>30 >20 >10 >5 all

Title	Phosphatidylinositol diphosphate binding by ESCRT-III filaments.
Journal, issue, pages	Proc Natl Acad Sci U S A, Vol. 123, Issue 27, Page e2616668123, Year 2026
Publish date	Jul 7, 2026
Authors	Akram Alian / John McCullough / Frank R Moss / Nathaniel Talledge / Arshad Mohammed / Cecilia D Gerstner / Jacob A Dalluge / Elliott L Paine / Omar Davulcu / Chi-Lun Chang / Adam Frost / Wesley I Sundquist /
PubMed Abstract	Different inositol phospholipids (PIPs) distribute to distinct subcellular organelles, creating an addressing system that dictates the sites of action of PIP-binding proteins, including components of ...Different inositol phospholipids (PIPs) distribute to distinct subcellular organelles, creating an addressing system that dictates the sites of action of PIP-binding proteins, including components of the Endosomal Sorting Complexes Required for Transport (ESCRT). The ESCRT machinery is recruited to remodel many different cellular membranes through combinatorial binding interactions made by the early-acting ESCRT-I and ESCRT-II complexes with PIPs, ubiquitin modifications, and membrane-specific adaptors. Membrane remodeling, constriction, and fission are then mediated by membrane-associated filaments formed by subunits of the late-acting ESCRT-III complexes, together with their associated VPS4 AAA ATPases. Here, we describe two different classes of helical ESCRT-III filaments that can surround and tubulate membranes containing PIP 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 or PI(3,5)P headgroups within a basic pocket formed at the junction of three IST1 subunits, and our structures reveal how the pocket can accommodate either PIP 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 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 lipids can promote ESCRT-III filament assembly and membrane remodeling, and define the molecular contacts that underlie specific ESCRT-III/PIP interactions.
External links	Proc Natl Acad Sci U S A / PubMed:42378278 / PubMed Central
Methods	EM (helical sym.)
Resolution	2.0 - 3.3 Å
Structure data	77057 13gh EMDB-77057, PDB-13gh: IST1 bound to PI(3,5)P2 containing membrane Method: EM (helical sym.) / Resolution: 2.56 Å 77058 13gj EMDB-77058, PDB-13gj: IST1 bound to PI(4,5)P2 containing membrane Method: EM (helical sym.) / Resolution: 2.0 Å 77060 13gm EMDB-77060, PDB-13gm: CHMP1A bound to PI(4,5)P2 containing membrane Method: EM (helical sym.) / Resolution: 3.3 Å
Chemicals	ChemComp-EUJ: (2R)-3-{[(S)-hydroxy{[(1S,2R,3R,4S,5S,6R)-2,4,6-trihydroxy-3,5-bis(phosphonooxy)cyclohexyl]oxy}phosphoryl]oxy}propane-1,2-diyl dioctanoate ChemComp-HOH: WATER ChemComp-PIO: [(2R)-2-octanoyloxy-3-[oxidanyl-[(1R,2R,3S,4R,5R,6S)-2,3,6-tris(oxidanyl)-4,5-diphosphonooxy-cyclohexyl]oxy-phosphoryl]oxy-propyl] octanoate
Source	homo sapiens (human)
Keywords	LIPID BINDING PROTEIN / ESCRT / ESCRT-III / PIP2 / PI(3 / 5)P2 / endosomal / cytokinesis / PI(4 / CHMP1A