2023
Twist response of actin filaments
Bibeau J, Pandit N, Gray S, Nejad N, Sindelar C, Cao W, De La Cruz E. Twist response of actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2023, 120: e2208536120. PMID: 36656858, PMCID: PMC9942836, DOI: 10.1073/pnas.2208536120.Peer-Reviewed Original Research
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
Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches
Pandit NG, Cao W, Bibeau J, Johnson-Chavarria EM, Taylor EW, Pollard TD, De La Cruz EM. Force and phosphate release from Arp2/3 complex promote dissociation of actin filament branches. Proceedings Of The National Academy Of Sciences Of The United States Of America 2020, 117: 13519-13528. PMID: 32461373, PMCID: PMC7306818, DOI: 10.1073/pnas.1911183117.Peer-Reviewed Original ResearchConceptsActin filament branchesArp2/3 complexMother filamentFilament branchesTotal internal reflection fluorescence microscopyEssential cellular functionsMechanical forcesActin filament networkReflection fluorescence microscopyCellular functionsActin networkCell motilityComplex generatesActin filamentsArp2/3Filament networkFluorescence microscopyState 1Branch junctionsState 2FilamentsComplexesPhosphate releaseMuscle actinADPStructures 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 ResearchConceptsFilament 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
2019
Plastic Deformation and Fragmentation of Strained Actin Filaments
Schramm AC, Hocky GM, Voth GA, Martiel JL, De La Cruz EM. Plastic Deformation and Fragmentation of Strained Actin Filaments. Biophysical Journal 2019, 117: 453-463. PMID: 31301801, PMCID: PMC6697348, DOI: 10.1016/j.bpj.2019.06.018.Peer-Reviewed Original Research
2018
Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release
Wong EV, Gray S, Cao W, Montpetit R, Montpetit B, De La Cruz EM. Nup159 Weakens Gle1 Binding to Dbp5 But Does Not Accelerate ADP Release. Journal Of Molecular Biology 2018, 430: 2080-2095. PMID: 29782832, PMCID: PMC6003625, DOI: 10.1016/j.jmb.2018.05.025.Peer-Reviewed Original ResearchConceptsEssential DEAD-box proteinADP releaseDbp5's ATPase activityDEAD-box proteinsNucleotide exchange factorsDbp5 activityMRNA exportRNA metabolismExchange factorDbp5Cellular processesATPase cyclingNup159Gle1ATP affinityMechanochemical cycleATPase activityADPATP releaseDDX19NTPasesNucleoporinsDetailed characterizationRNARegulator
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 ResearchConceptsContinuum 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
2016
Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding Characteristics
Wang B, Boeckel GR, Huynh L, Nguyen L, Cao W, De La Cruz EM, Kaftan EJ, Ehrlich BE. Neuronal Calcium Sensor 1 Has Two Variants with Distinct Calcium Binding Characteristics. PLOS ONE 2016, 11: e0161414. PMID: 27575489, PMCID: PMC5004852, DOI: 10.1371/journal.pone.0161414.Peer-Reviewed Original ResearchConceptsNeuronal calcium sensor-1NCS-1Altered cell functionCell linesCalcium-dependent processesCalcium binding proteinNeurological diseasesFunctional changesLevel of expressionDrug potencyProtein expressionCell functionMRNA levelsHuman cell linesRelative expressionMost tissuesCell deathPrevious reportsMouse tissuesDifferent human cell linesCell growthFunctional roleBinding characteristicsFunctional differencesTissueCations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits
Hocky GM, Baker JL, Bradley MJ, Sinitskiy AV, De La Cruz EM, Voth GA. Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits. The Journal Of Physical Chemistry B 2016, 120: 4558-4567. PMID: 27146246, PMCID: PMC4959277, DOI: 10.1021/acs.jpcb.6b02741.Peer-Reviewed Original ResearchConceptsActin filamentsRegulatory proteinsD-loopSite-specific mutagenesisSpecific divalent cationsFilament severingStructural bioinformaticsAdjacent subunitsAccessible conformational spaceSubunit conformationActin subunitsKey structural elementsAmino acidsLarge-scale changesConformational spaceSubunitsFilament mechanical propertiesProteinFilamentsDivalent cationsMagnesium ionsMolecular dynamics simulationsConformationSitesCofilin
2015
Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments
Durer Z, McGillivary RM, Kang H, Elam WA, Vizcarra CL, Hanein D, De La Cruz EM, Reisler E, Quinlan ME. Metavinculin Tunes the Flexibility and the Architecture of Vinculin-Induced Bundles of Actin Filaments. Journal Of Molecular Biology 2015, 427: 2782-2798. PMID: 26168869, PMCID: PMC4540644, DOI: 10.1016/j.jmb.2015.07.005.Peer-Reviewed Original ResearchConceptsMetavinculin tail domainVinculin tail domainActin filamentsTail domainSevering activityCell-extracellular matrix junctionsF-actinC-terminal tail domainTotal internal reflection fluorescence microscopy experimentsLonger splice isoformsLimited proteolysis experimentsActin filament bundlesFluorescence microscopy experimentsMatrix junctionsSite-directed labelingSplice isoformsAbundant proteinsProteolysis experimentsMuscle cell functionFilament organizationVinculinFilament bundlesInterprotomer contactsCell functionFilament flexibility
2013
Regulation of Actin by Ion-Linked Equilibria
Kang H, Bradley MJ, Elam WA, De La Cruz EM. Regulation of Actin by Ion-Linked Equilibria. Biophysical Journal 2013, 105: 2621-2628. PMID: 24359734, PMCID: PMC3882474, DOI: 10.1016/j.bpj.2013.10.032.Peer-Reviewed Original ResearchCompetitive displacement of cofilin can promote actin filament severing
Elam WA, Kang H, De La Cruz EM. Competitive displacement of cofilin can promote actin filament severing. Biochemical And Biophysical Research Communications 2013, 438: 728-731. PMID: 23911787, PMCID: PMC3785092, DOI: 10.1016/j.bbrc.2013.07.109.Peer-Reviewed Original ResearchBiophysics of actin filament severing by cofilin
Elam WA, Kang H, De La Cruz EM. Biophysics of actin filament severing by cofilin. FEBS Letters 2013, 587: 1215-1219. PMID: 23395798, PMCID: PMC4079045, DOI: 10.1016/j.febslet.2013.01.062.Peer-Reviewed Original ResearchMolecular 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
2011
Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate
Wu X, Bradley MJ, Cai Y, Kümmel D, De La Cruz EM, Barr FA, Reinisch KM. Insights regarding guanine nucleotide exchange from the structure of a DENN-domain protein complexed with its Rab GTPase substrate. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: 18672-18677. PMID: 22065758, PMCID: PMC3219131, DOI: 10.1073/pnas.1110415108.Peer-Reviewed Original ResearchMeSH KeywordsBinding SitesBiological TransportCrystallography, X-RayDeath Domain Receptor Signaling Adaptor ProteinsGuanineGuanine Nucleotide Exchange FactorsHumansKineticsNucleotidesProtein BindingProtein Structure, SecondaryProtein Structure, TertiaryRab GTP-Binding ProteinsRab1 GTP-Binding ProteinsConceptsGuanine nucleotide exchange factorsDENN domain proteinsMembrane traffic pathwaysNucleotide exchange factorsGDP-bound formGTP-bound formSwitch regions IHigher eukaryotesRab GTPasesGEF familyEukaryotic cellsTraffic pathwaysExchange factorSwitch INucleotide bindingKey regulatorConformational changesFirst structureNovel insightsRab35ProteinDENND1BEukaryotesRegion IGTPasesDirect Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin
Shiroguchi K, Chin HF, Hannemann DE, Muneyuki E, De La Cruz EM, Kinosita K. Direct Observation of the Myosin Va Recovery Stroke That Contributes to Unidirectional Stepping along Actin. PLOS Biology 2011, 9: e1001031. PMID: 21532738, PMCID: PMC3075224, DOI: 10.1371/journal.pbio.1001031.Peer-Reviewed Original Research
2010
The Kinetics of Cooperative Cofilin Binding Reveals Two States of the Cofilin-Actin Filament
De La Cruz EM, Sept D. The Kinetics of Cooperative Cofilin Binding Reveals Two States of the Cofilin-Actin Filament. Biophysical Journal 2010, 98: 1893-1901. PMID: 20441753, PMCID: PMC2862197, DOI: 10.1016/j.bpj.2010.01.023.Peer-Reviewed Original ResearchActin filament remodeling by actin depolymerization factor/cofilin
Pfaendtner J, De La Cruz EM, Voth GA. Actin filament remodeling by actin depolymerization factor/cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 7299-7304. PMID: 20368459, PMCID: PMC2867716, DOI: 10.1073/pnas.0911675107.Peer-Reviewed Original ResearchConceptsActin depolymerization factorSubunit interactionsCofilin bindingActin filamentsADF/cofilinFactor/cofilinLong-pitch helixHelix monomersNeighboring subunitMolecular basisSevering proteinHydrophobic loopConformational dynamicsSubdomain 1Subdomain 2Loop movesTriggers reorganizationCofilinFilament flexibilityFilamentsNative filamentsDNaseFilament contactsAtom simulationsBinding
2009
Kinetic Analysis of the Guanine Nucleotide Exchange Activity of TRAPP, a Multimeric Ypt1p Exchange Factor
Chin HF, Cai Y, Menon S, Ferro-Novick S, Reinisch KM, De La Cruz EM. Kinetic Analysis of the Guanine Nucleotide Exchange Activity of TRAPP, a Multimeric Ypt1p Exchange Factor. Journal Of Molecular Biology 2009, 389: 275-288. PMID: 19361519, PMCID: PMC2770256, DOI: 10.1016/j.jmb.2009.03.068.Peer-Reviewed Original ResearchConceptsMembrane trafficExchange factorGuanine nucleotide exchange activityRab GTPase Ypt1pLarge multimeric assembliesNucleotide exchange activityThermodynamic linkage analysisWeak thermodynamic couplingTRAPP complexesStable ternary complexTRAPP subunitsGEF activityYpt1pNucleotide bindingMultimeric assembliesNucleotide exchangeNucleotide dissociationNucleotide affinityLinkage analysisIndependent pathwaysGEF systemTernary complexExchange activityTRAPPOverall net change