2025
High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory
Chavali S, Carman P, Shuman H, Ostap E, Sindelar C. High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2415457122. PMID: 40014570, PMCID: PMC11892617, DOI: 10.1073/pnas.2415457122.Peer-Reviewed Original ResearchConceptsN-terminal extensionATP bindingRegulating ATP bindingADP releaseClass I myosinsLever arm swingStructure of myosinCryo-EM structureHigh-resolution structuresMembrane-bound vesiclesActin interfaceMyosin superfamilyMyosin familyActin filamentsAbsence of ADPMembrane remodelingNucleotide pocketMotile behaviorMyo1cPlasma membraneBiological functionsActinCryo-EM dataMotor domainMyosin
2024
Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2354. PMID: 38491023, PMCID: PMC10943100, DOI: 10.1038/s41467-024-46804-9.Peer-Reviewed Original ResearchCryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2059. PMID: 38448439, PMCID: PMC10918085, DOI: 10.1038/s41467-024-46179-x.Peer-Reviewed Original ResearchConceptsArp2/3 complexActin filamentsCryo-EM structureMother filamentDaughter filamentArp2/3 complex nucleates branched actin filamentsActin filament branchingBranched actin filamentsDissociation of PiADP-PiFilament branchingOrganelle movementADP stateBranch junctionsArp3A-resolutionActinArp2/3ADP-BeFxFilamentsADPPhosphate releaseFilament mechanismArp2Organelles
2018
High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing
Mentes A, Huehn A, Liu X, Zwolak A, Dominguez R, Shuman H, Ostap EM, Sindelar CV. High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 1292-1297. PMID: 29358376, PMCID: PMC5819444, DOI: 10.1073/pnas.1718316115.Peer-Reviewed Original ResearchConceptsN-terminal subdomainHigh-resolution cryo-EM structuresADP stateNear-atomic resolution structuresCryo-EM structureCryo-electron microscopyHigh-resolution structuresIsoform-dependent mannerFilamentous actinResolution structureStructural basisMyosin IBActin filamentsStructural diversityRelease pathwayADP releaseActinPointed endPotent stabilizerMyosin
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