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 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
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 ResearchConceptsCofilin-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
2016
Architecture and Connectivity Govern Actin Network Contractility
Ennomani H, Letort G, Guérin C, Martiel JL, Cao W, Nédélec F, De La Cruz EM, Théry M, Blanchoin L. Architecture and Connectivity Govern Actin Network Contractility. Current Biology 2016, 26: 616-626. PMID: 26898468, PMCID: PMC4959279, DOI: 10.1016/j.cub.2015.12.069.Peer-Reviewed Original Research
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
Competitive 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 Research
2012
Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness
Kang H, Bradley MJ, McCullough BR, Pierre A, Grintsevich EE, Reisler E, De La Cruz EM. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16923-16927. PMID: 23027950, PMCID: PMC3479481, DOI: 10.1073/pnas.1211078109.Peer-Reviewed Original ResearchConceptsCation-binding sitesActin assemblyEukaryotic biologyLong-pitch helixActin functionSalt-dependent effectsCell divisionCell motilityActin polymerizationFilament assemblyAdjacent subunitsIntracellular transportActin filamentsPhysiological salt concentrationsActin monomersCellular shapeNonspecific ionic strength effectsDiscrete sitesActin 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 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
2010
Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11
Kucera K, Koblansky AA, Saunders LP, Frederick KB, De La Cruz EM, Ghosh S, Modis Y. Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11. Journal Of Molecular Biology 2010, 403: 616-629. PMID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCrystallography, X-RayDNA PrimersImmunity, InnateIn Vitro TechniquesMacrophages, PeritonealMiceMice, KnockoutModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPlasmodium falciparumProfilinsProtein Structure, SecondaryProtozoan ProteinsRabbitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionStatic ElectricityToll-Like ReceptorsToxoplasmaConceptsAcidic loopToll-like receptor 11Β-hairpinLong β-hairpinApicomplexan parasite Cryptosporidium parvumActin-binding surfaceFilament barbed endsStructure-based analysisYeast profilinGondii profilinProfilin mutantsGliding motilityParasite Cryptosporidium parvumT. gondii profilinNucleotide exchangeToxoplasma gondii profilinRabbit actinPlasmodium falciparum resultsActin polymerizationApicomplexan protozoaHomologous loopBarbed endsHost cellsIL-12 secretionInnate immune responseRobust processivity of myosin V under off-axis loads
Oguchi Y, Mikhailenko SV, Ohki T, Olivares AO, De La Cruz EM, Ishiwata S. Robust processivity of myosin V under off-axis loads. Nature Chemical Biology 2010, 6: 300-305. PMID: 20228794, PMCID: PMC2917589, DOI: 10.1038/nchembio.322.Peer-Reviewed Original Research
2008
Load-dependent ADP binding to myosins V and VI: Implications for subunit coordination and function
Oguchi Y, Mikhailenko SV, Ohki T, Olivares AO, De La Cruz EM, Ishiwata S. Load-dependent ADP binding to myosins V and VI: Implications for subunit coordination and function. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 7714-7719. PMID: 18509050, PMCID: PMC2409399, DOI: 10.1073/pnas.0800564105.Peer-Reviewed Original ResearchCofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics
McCullough BR, Blanchoin L, Martiel JL, De La Cruz EM. Cofilin Increases the Bending Flexibility of Actin Filaments: Implications for Severing and Cell Mechanics. Journal Of Molecular Biology 2008, 381: 550-558. PMID: 18617188, PMCID: PMC2753234, DOI: 10.1016/j.jmb.2008.05.055.Peer-Reviewed Original ResearchWidely Distributed Residues in Thymosin β4 Are Critical for Actin Binding
Au JK, Olivares AO, Henn A, Cao W, Safer D, De La Cruz EM. Widely Distributed Residues in Thymosin β4 Are Critical for Actin Binding. Biochemistry 2008, 47: 4181-4188. PMID: 18327913, PMCID: PMC2587058, DOI: 10.1021/bi701769u.Peer-Reviewed Original ResearchConceptsActin Binding AffinityActin bindingProline residuesHydrophobic residuesAlanine residuesLysine residuesPro27Thymosin beta4Actin monomersPro29MutagenesisHydrophobic contactsLeu28Slow association rateResiduesLys19Thymosin β4Ile34Tbeta4Lys18Binding affinitiesTwo-step mechanismAssociation ratePro4Cis-trans isomerization
2007
Contributions from All Over
AU JK, DE LA CRUZ EM, SAFER D. Contributions from All Over. Annals Of The New York Academy Of Sciences 2007, 1112: 38-44. PMID: 17468230, DOI: 10.1196/annals.1415.015.Peer-Reviewed Original ResearchConceptsProline residuesActin bindingWild-type complexHydrophobic contactsSite-directed mutagenesisStrong actin bindingHydrophobic residuesAlanine residuesCysteine 374Slow association rateRate of associationResiduesMutantsComplex variesTbeta4Association rateSulfo-1BindingCis-trans isomerizationKinetic basisComplexesPro27Pro29Lys19Mutagenesis
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
2005
Thymosin β4 Induces a Conformational Change in Actin Monomers
Dedova IV, Nikolaeva OP, Safer D, De La Cruz EM, dos Remedios CG. Thymosin β4 Induces a Conformational Change in Actin Monomers. Biophysical Journal 2005, 90: 985-992. PMID: 16272441, PMCID: PMC1367123, DOI: 10.1529/biophysj.105.063081.Peer-Reviewed Original ResearchAcrylamideActinsAdenosine TriphosphateAnimalsCalorimetry, Differential ScanningCysteineElectrophoresis, Polyacrylamide GelFluorescence Resonance Energy TransferHot TemperatureKineticsLysineModels, MolecularMolecular ConformationNucleotidesProtein BindingProtein ConformationProtein Structure, TertiaryPurinesRabbitsSolventsSpectrometry, FluorescenceTemperatureThymosinVertebrate Myosin VIIb Is a High Duty Ratio Motor Adapted for Generating and Maintaining Tension*
Henn A, De La Cruz EM. Vertebrate Myosin VIIb Is a High Duty Ratio Motor Adapted for Generating and Maintaining Tension*. Journal Of Biological Chemistry 2005, 280: 39665-39676. PMID: 16186105, DOI: 10.1074/jbc.m507667200.Peer-Reviewed Original ResearchConceptsClass VII myosinMyosin VIIbActin filament concentrationUnique cellular functionsInner ear hair cellsCatalytic motor domainEar hair cellsActin filament bundlesNon-muscle myosinSteady-state ATPase activityActin cytoskeletonHigh conservationCellular functionsMyosin VIIa functionCDNA libraryActin bindingDeafness phenotypeMembrane surface receptorsATPase cycleEnzymatic propertiesSurface receptorsFilament bundlesIntestinal brush borderMolecular motorsQuantitative equilibrium