2024
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. 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 ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2-3 ComplexActinsCryoelectron MicroscopyCytoskeletonPhosphatesConceptsArp2/3 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
2021
Clusters of a Few Bound Cofilins Sever Actin Filaments
Bibeau JP, Gray S, De La Cruz EM. Clusters of a Few Bound Cofilins Sever Actin Filaments. Journal Of Molecular Biology 2021, 433: 166833. PMID: 33524412, PMCID: PMC8689643, DOI: 10.1016/j.jmb.2021.166833.Peer-Reviewed Original Research
2020
Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments
Huehn AR, Bibeau JP, Schramm AC, Cao W, De La Cruz EM, Sindelar CV. Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 1478-1484. PMID: 31900364, PMCID: PMC6983403, DOI: 10.1073/pnas.1915987117.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin Depolymerizing FactorsAnimalsBinding SitesCryoelectron MicroscopyHumansPhosphorylationProtein BindingRabbitsConceptsFilament severingActin filamentsSevering activityCofilin/ADF familyActin conformational changesActin filament severingFilament-severing activityCryo-electron microscopy dataSevers actin filamentsWeak severing activityUnique binding modeCofilin clustersActin structuresCofilin bindingCofilin-decorated segmentsCofilinMolecular understandingBarbed endsConformational changesCooperative bindingBinding cooperativityFilament endsPositive cooperativityBinding modesSevering
2018
The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments
Huehn A, Cao W, Elam WA, Liu X, De La Cruz EM, Sindelar CV. The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. Journal Of Biological Chemistry 2018, 293: 5377-5383. PMID: 29463680, PMCID: PMC5900768, DOI: 10.1074/jbc.ac118.001843.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin Depolymerizing FactorsAnimalsCryoelectron MicroscopyProtein Structure, QuaternaryRabbitsConceptsCofilin-decorated segmentsConformational changesCofilin/ADF proteinsActin-remodeling proteinsBind actin filamentsActin filament interactionsCofilin-induced changesEffects of cofilinCooperative conformational changesProtein occupancyADF proteinsCellular processesCell divisionStructure-based methodsCryo-EMActin segmentsIntracellular transportActin filamentsFilament twistCooperative bindingCofilinTwist changesActinFluorophore labelingSubunits
2017
Phosphomimetic S3D cofilin binds but only weakly severs actin filaments
Elam WA, Cao W, Kang H, Huehn A, Hocky GM, Prochniewicz E, Schramm AC, Negrón K, Garcia J, Bonello TT, Gunning PW, Thomas DD, Voth GA, Sindelar CV, De La Cruz EM. Phosphomimetic S3D cofilin binds but only weakly severs actin filaments. Journal Of Biological Chemistry 2017, 292: 19565-19579. PMID: 28939776, PMCID: PMC5712599, DOI: 10.1074/jbc.m117.808378.Peer-Reviewed Original ResearchConceptsActin bindingWild-type cofilinActin filament severingHigh cooperativitySubstitution of serineCofilin bindsActin cytoskeletonProtein cofilinCell divisionSer-3Filament severingAtom molecular dynamics simulationsSubunit interactionsN-terminusCofilinBiological processesActin filamentsTime-resolved phosphorescence anisotropyElectron cryomicroscopyRapid remodelingPhosphorylationSeveringFilament mechanical propertiesActin segmentsFilamentsActin Filament Strain Promotes Severing and Cofilin Dissociation
Schramm AC, Hocky GM, Voth GA, Blanchoin L, Martiel JL, De La Cruz EM. Actin Filament Strain Promotes Severing and Cofilin Dissociation. Biophysical Journal 2017, 112: 2624-2633. PMID: 28636918, PMCID: PMC5479148, DOI: 10.1016/j.bpj.2017.05.016.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin Depolymerizing FactorsActinsCryoelectron MicroscopyElasticityMolecular Dynamics SimulationProtein BindingRotationConceptsContinuum mechanics modelStrain energy distributionMechanical propertiesMechanics modelFilament twistingEnhanced spatial resolutionFilament mechanical propertiesElastic energyTorsional rigidityShape deformationSpatial resolutionContinuum modelTorsional flexibilityFilament bendingCofilactin filamentsDynamics simulationsMolecular dynamics simulationsBucklingCofilin-decorated segmentsDeformationBendingBoundariesEnergy distributionLoadFilament model
2014
Site-specific cation release drives actin filament severing by vertebrate cofilin
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 17821-17826. PMID: 25468977, PMCID: PMC4273407, DOI: 10.1073/pnas.1413397111.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonCationsCell MovementChromatography, AffinityCofilin 1Cryoelectron MicroscopyHumansModels, MolecularSaccharomyces cerevisiaeConceptsFilament severingActin filamentsActin filament severingKey regulatory functionsConcentration of endsActin filament fragmentationEukaryotic cellsCation-binding sitesProtein cofilinDeletion mutantsS. cerevisiaeSubunit exchangeFilament turnoverActin polymerizationEssential functionsSite-specific interactionsCofilinMolecular mechanismsAssembly dynamicsRegulatory functionsActin moleculesFilament fragmentationFilament structureSustained motilitySevering
2013
Molecular Origins of Cofilin-Linked Changes in Actin Filament Mechanics
Fan J, Saunders MG, Haddadian EJ, Freed KF, De La Cruz EM, Voth GA. Molecular Origins of Cofilin-Linked Changes in Actin Filament Mechanics. Journal Of Molecular Biology 2013, 425: 1225-1240. PMID: 23352932, PMCID: PMC3740545, DOI: 10.1016/j.jmb.2013.01.020.Peer-Reviewed Original Research