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 mechanismArp2OrganellesDistinct functional constraints driving conservation of the cofilin N-terminal regulatory tail
Sexton J, Potchernikov T, Bibeau J, Casanova-Sepúlveda G, Cao W, Lou H, Boggon T, De La Cruz E, Turk B. Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail. Nature Communications 2024, 15: 1426. PMID: 38365893, PMCID: PMC10873347, DOI: 10.1038/s41467-024-45878-9.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin Depolymerizing FactorsActinsCofilin 1HumansLim KinasesPhosphorylationSaccharomyces cerevisiaeConceptsN-terminal regionActin bindingSequence requirementsLIM kinaseAnalysis of individual variantsInactivates cofilinS. cerevisiaeRegulatory tailFamily proteinsActin depolymerizationPhosphorylation sitesKinase recognitionSequence variantsInhibitory phosphorylationCofilinN-terminusIndividual variantsFunctional constraintsActinDisordered sequencesPhosphorylationSequenceBiochemical analysisSequence constraintsKinase
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
Structural basis of fast- and slow-severing actin–cofilactin boundaries
Hocky GM, Sindelar CV, Cao W, Voth GA, De La Cruz EM. Structural basis of fast- and slow-severing actin–cofilactin boundaries. Journal Of Biological Chemistry 2021, 296: 100337. PMID: 33508320, PMCID: PMC7961102, DOI: 10.1016/j.jbc.2021.100337.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 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
2019
Active cargo positioning in antiparallel transport networks
Richard M, Blanch-Mercader C, Ennomani H, Cao W, De La Cruz EM, Joanny JF, Jülicher F, Blanchoin L, Martin P. Active cargo positioning in antiparallel transport networks. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 14835-14842. PMID: 31289230, PMCID: PMC6660773, DOI: 10.1073/pnas.1900416116.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsBiological TransportMotionMyosinsSingle Molecule ImagingStochastic Processes
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 segmentsFilaments
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 motilitySeveringMulti-Platform Compatible Software for Analysis of Polymer Bending Mechanics
Graham JS, McCullough BR, Kang H, Elam WA, Cao W, De La Cruz EM. Multi-Platform Compatible Software for Analysis of Polymer Bending Mechanics. PLOS ONE 2014, 9: e94766. PMID: 24740323, PMCID: PMC3989245, DOI: 10.1371/journal.pone.0094766.Peer-Reviewed Original Research
2012
Actin Network Architecture Can Determine Myosin Motor Activity
Reymann AC, Boujemaa-Paterski R, Martiel JL, Guérin C, Cao W, Chin HF, De La Cruz EM, Théry M, Blanchoin L. Actin Network Architecture Can Determine Myosin Motor Activity. Science 2012, 336: 1310-1314. PMID: 22679097, PMCID: PMC3649007, DOI: 10.1126/science.1221708.Peer-Reviewed Original ResearchPlus‐end directed myosins accelerate actin filament sliding by single‐headed myosin VI
Ramamurthy B, Cao W, De La Cruz EM, Mooseker MS. Plus‐end directed myosins accelerate actin filament sliding by single‐headed myosin VI. Cytoskeleton 2012, 69: 59-69. PMID: 22213699, PMCID: PMC3327287, DOI: 10.1002/cm.21002.Peer-Reviewed Original Research
2011
Actin Filament Dynamics in the Actomyosin VI Complex Is Regulated Allosterically by Calcium–Calmodulin Light Chain
Prochniewicz E, Pierre A, McCullough BR, Chin HF, Cao W, Saunders LP, Thomas DD, De La Cruz EM. Actin Filament Dynamics in the Actomyosin VI Complex Is Regulated Allosterically by Calcium–Calmodulin Light Chain. Journal Of Molecular Biology 2011, 413: 584-592. PMID: 21910998, PMCID: PMC3633491, DOI: 10.1016/j.jmb.2011.08.058.Peer-Reviewed Original ResearchConceptsActin filament dynamicsMyosin VIFilament dynamicsMicrosecond dynamicsCaM-dependent mannerCalmodulin light chainsLight chainActin bindingActin filamentsDependent CaMIQ domainCaM-dependent regulationFluorescence microscopyEnzymatic activityTransient phosphorescence anisotropyATP utilizationFinal anisotropyMicrosecond rotational dynamicsPhosphorescence anisotropyMyosinStructural dynamicsAnisotropy decaySuch modulationActinRegulationCofilin-Linked Changes in Actin Filament Flexibility Promote Severing
McCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM. Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing. Biophysical Journal 2011, 101: 151-159. PMID: 21723825, PMCID: PMC3127193, DOI: 10.1016/j.bpj.2011.05.049.Peer-Reviewed Original Research
2006
Energetics and Kinetics of Cooperative Cofilin–Actin Filament Interactions
Cao W, Goodarzi JP, De La Cruz EM. Energetics and Kinetics of Cooperative Cofilin–Actin Filament Interactions. Journal Of Molecular Biology 2006, 361: 257-267. PMID: 16843490, DOI: 10.1016/j.jmb.2006.06.019.Peer-Reviewed Original Research