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	Choreography of rapid actin filament disassembly by coronin, cofilin, and AIP1.
Journal, issue, pages	Cell, Vol. 188, Issue 24, Page 6845-6860.e27, Year 2025
Publish date	Nov 26, 2025
Authors	Wout Oosterheert / Micaela Boiero Sanders / Oliver Hofnagel / Peter Bieling / Stefan Raunser /
PubMed Abstract	Rapid remodeling of actin filament (F-actin) networks is essential for the movement and morphogenesis of eukaryotic cells. The conserved actin-binding proteins coronin, cofilin, and actin-interacting ...Rapid remodeling of actin filament (F-actin) networks is essential for the movement and morphogenesis of eukaryotic cells. The conserved actin-binding proteins coronin, cofilin, and actin-interacting protein 1 (AIP1) act in synergy to promote rapid F-actin network disassembly, but the underlying mechanisms have remained elusive. Here, using cryo-electron microscopy (cryo-EM), we uncover the concerted molecular actions of coronin, cofilin, and AIP1 that lead to actin filament aging and severing. We find that the cooperative binding of coronin allosterically promotes inorganic phosphate release from F-actin and induces filament undertwisting, thereby priming the filament for cofilin binding. Cofilin then displaces coronin from the filament via a strand-restricted cooperative binding mechanism. The resulting cofilactin serves as a high-affinity platform for AIP1, which induces severing by acting as a clamp that disrupts inter-subunit filament contacts. In this "molecular squeezing" mechanism, AIP1 and not cofilin is responsible for filament severing. Our work redefines the role of key disassembly factors in actin dynamics.
External links	Cell / PubMed:41075793
Methods	EM (single particle) / EM (helical sym.)
Resolution	2.18 - 4.62 Å
Structure data	53093 9qew EMDB-53093, PDB-9qew: Cryo-EM structure of the undecorated actin filament in the ADP-Pi state. Method: EM (single particle) / Resolution: 2.18 Å 53094 9qey EMDB-53094, PDB-9qey: Cryo-EM structure of the actin filament bound by a single Coronin-1B molecule. Method: EM (single particle) / Resolution: 2.74 Å 53096 9qf2 EMDB-53096, PDB-9qf2: Cryo-EM structure of the fully Coronin-1B-decorated actin filament in the ADP state. Method: EM (single particle) / Resolution: 2.42 Å 53105 9qfb EMDB-53105, PDB-9qfb: Cryo-EM structure of the fully Coronin-1B-decorated actin filament in the ADP state. Method: EM (helical sym.) / Resolution: 2.74 Å 53106 9qfd EMDB-53106, PDB-9qfd: Cryo-EM structure of the fully cofilin-1-decorated actin filament (cofilactin) Method: EM (helical sym.) / Resolution: 2.61 Å 53107 9qfe EMDB-53107, PDB-9qfe: Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1 on separate actin strands Method: EM (single particle) / Resolution: 3.12 Å 53108 9qfg EMDB-53108, PDB-9qfg: Cryo-EM structure of the actin filament hetero-decorated by Coronin-1 and Cofilin-1, strand boundary Method: EM (single particle) / Resolution: 3.49 Å 53110 9qfj EMDB-53110, PDB-9qfj: Cryo-EM structure of the cofilactin filament core at 2.3 Angstrom resolution. Method: EM (single particle) / Resolution: 2.31 Å EMDB-53111: Cryo-EM reconstruction of the Coronin-1B-decorated actin filament bound by two Cofilin-1 molecules (crosslinked) Method: EM (single particle) / Resolution: 4.43 Å EMDB-53112: Cryo-EM reconstruction of the Coronin-1B-decorated actin filament bound by three Cofilin-1 molecules (crosslinked) Method: EM (single particle) / Resolution: 4.36 Å EMDB-53113: Cryo-EM reconstruction of the Coronin-1B-decorated actin filament bound by four Cofilin-1 molecules (crosslinked) Method: EM (single particle) / Resolution: 4.33 Å 53114 9qfk EMDB-53114, PDB-9qfk: Cryo-EM structure of the Coronin-1B-decorated actin filament bound by one Cofilin-1 molecule (crosslinked) Method: EM (single particle) / Resolution: 3.99 Å EMDB-53118: Cryo-EM reconstruction of the cofilactin filament core bound by AIP1 Method: EM (single particle) / Resolution: 4.62 Å 53119 9qfo EMDB-53119, PDB-9qfo: Cryo-EM structure of the cofilactin filament pointed end Method: EM (single particle) / Resolution: 2.96 Å 53121 9qfq EMDB-53121, PDB-9qfq: Cryo-EM structure of the cofilactin barbed end bound by AIP1 Method: EM (single particle) / Resolution: 2.76 Å 53122 9qfw EMDB-53122, PDB-9qfw: Cryo-EM structure of the cofilactin barbed end bound by two AIP1 molecules Method: EM (single particle) / Resolution: 3.16 Å
Chemicals	ChemComp-ADP: ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying moleculeYM ChemComp-MG: Unknown entry ChemComp-PO4: PHOSPHATE ION ChemComp-HOH*: WATER
Source	homo sapiens (human)
Keywords	STRUCTURAL PROTEIN / actin / filament / cytoskeleton / coronin / cofilin / pointed end / AIP1 / barbed end