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 actinADP
2018
Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments
Katkar HH, Davtyan A, Durumeric AEP, Hocky GM, Schramm AC, De La Cruz EM, Voth GA. Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments. Biophysical Journal 2018, 115: 1589-1602. PMID: 30249402, PMCID: PMC6260209, DOI: 10.1016/j.bpj.2018.08.034.Peer-Reviewed Original ResearchActin CytoskeletonActinsAdenosine DiphosphateAdenosine TriphosphateHumansHydrolysisKineticsPhosphatesNup159 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
2012
NPP4 is a procoagulant enzyme on the surface of vascular endothelium
Albright RA, Chang WC, Robert D, Ornstein DL, Cao W, Liu L, Redick ME, Young JI, De La Cruz EM, Braddock DT. NPP4 is a procoagulant enzyme on the surface of vascular endothelium. Blood 2012, 120: 4432-4440. PMID: 22995898, PMCID: PMC4017314, DOI: 10.1182/blood-2012-04-425215.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine DiphosphateAdultAnimalsBlood CoagulationCoagulantsCyclic Nucleotide Phosphodiesterases, Type 4Dinucleoside PhosphatesEndothelium, VascularFluorescent Antibody TechniqueHumansHydrolysisIn Vitro TechniquesInsectaPhosphoric Diester HydrolasesPlatelet AggregationPyrophosphatasesTissue DistributionConceptsPlatelet dense granule componentsNucleotide pyrophosphatase/phosphodiesteraseRelease of ADPUncharacterized enzymesPyrophosphatase/phosphodiesteraseGranule componentsEnzymatic basisRapid disaggregationDense granule releasePlatelet aggregationExtracellular spaceAp3AConcentration-dependent mannerEnzymeGranule releaseVascular endotheliumADPProcoagulant enzymeADP receptorActivationAggregationMutants
2011
Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins
Cao W, Coman MM, Ding S, Henn A, Middleton ER, Bradley MJ, Rhoades E, Hackney DD, Pyle AM, De La Cruz EM. Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins. Journal Of Molecular Biology 2011, 409: 399-414. PMID: 21501623, PMCID: PMC3125984, DOI: 10.1016/j.jmb.2011.04.004.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine DiphosphateAdenosine TriphosphatasesDEAD-box RNA HelicasesIntronsRNASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThermodynamicsConceptsGroup II intronsWeak RNARNA bindingDEAD-box RNA helicase proteinATP hydrolysisBiochemical intermediatesDEAD-box proteinsRNA helicase proteinStrong RNA bindingStable RNA duplexAbsence of nucleotideATP utilizationStrong thermodynamic couplingFunctional diversityIntron splicingStrong RNAIntron foldingVivo splicingHelicase proteinMRNA translationMss116ATPase cyclingVivo functionBiological roleADP state
2010
Robust 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 ResearchPathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA
Henn A, Cao W, Licciardello N, Heitkamp SE, Hackney DD, De La Cruz EM. Pathway of ATP utilization and duplex rRNA unwinding by the DEAD-box helicase, DbpA. Proceedings Of The National Academy Of Sciences Of The United States Of America 2010, 107: 4046-4050. PMID: 20160110, PMCID: PMC2840157, DOI: 10.1073/pnas.0913081107.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 ResearchEffects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability
Frederick KB, Sept D, De La Cruz EM. Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability. Journal Of Molecular Biology 2008, 378: 540-550. PMID: 18374941, PMCID: PMC2424216, DOI: 10.1016/j.jmb.2008.02.022.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonAdenosine DiphosphateAdenosine TriphosphateHydrolysisSolutionsSurface PropertiesThermodynamicsConceptsADP-actin filamentsFilament stabilityCell structure maintenanceFundamental cellular processesADP-actinADP-F-actinSolution crowdingCellular processesAllosteric regulatorsMolecular basisRegulatory proteinsActin polymerizationATP hydrolysisActin activityNucleotide hydrolysisFilament subunitsEnergetic basisIntracellular conditionsStructure maintenanceSubunit dissociationStability of ATPATPConcentration-dependent mannerStructural differencesForce generation
2005
Vertebrate 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 equilibriumHolding the reins on Myosin V
Olivares AO, De La Cruz EM. Holding the reins on Myosin V. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 13719-13720. PMID: 16172373, PMCID: PMC1236595, DOI: 10.1073/pnas.0507068102.Peer-Reviewed Original ResearchThermodynamics of Nucleotide Binding to Actomyosin V and VI: A Positive Heat Capacity Change Accompanies Strong ADP Binding †
Robblee JP, Cao W, Henn A, Hannemann DE, De La Cruz EM. Thermodynamics of Nucleotide Binding to Actomyosin V and VI: A Positive Heat Capacity Change Accompanies Strong ADP Binding †. Biochemistry 2005, 44: 10238-10249. PMID: 16042401, DOI: 10.1021/bi050232g.Peer-Reviewed Original ResearchMagnesium, ADP, and Actin Binding Linkage of Myosin V: Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States †
Hannemann DE, Cao W, Olivares AO, Robblee JP, De La Cruz EM. Magnesium, ADP, and Actin Binding Linkage of Myosin V: Evidence for Multiple Myosin V−ADP and Actomyosin V−ADP States †. Biochemistry 2005, 44: 8826-8840. PMID: 15952789, DOI: 10.1021/bi0473509.Peer-Reviewed Original Research
2004
Mechanochemical coupling of two substeps in a single myosin V motor
Uemura S, Higuchi H, Olivares AO, De La Cruz EM, Ishiwata S. Mechanochemical coupling of two substeps in a single myosin V motor. Nature Structural & Molecular Biology 2004, 11: 877-883. PMID: 15286720, DOI: 10.1038/nsmb806.Peer-Reviewed Original ResearchMechanism of Nucleotide Binding to Actomyosin VI EVIDENCE FOR ALLOSTERIC HEAD-HEAD COMMUNICATION*
Robblee JP, Olivares AO, De La Cruz EM. Mechanism of Nucleotide Binding to Actomyosin VI EVIDENCE FOR ALLOSTERIC HEAD-HEAD COMMUNICATION*. Journal Of Biological Chemistry 2004, 279: 38608-38617. PMID: 15247304, DOI: 10.1074/jbc.m403504200.Peer-Reviewed Original ResearchActinsActomyosinAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAllosteric SiteAnimalsCell LineDose-Response Relationship, DrugHydrogen-Ion ConcentrationInsectaKineticsModels, BiologicalModels, ChemicalModels, StatisticalMuscle, SkeletalMyosin Heavy ChainsNucleotidesProtein BindingPyrenesRabbitsTime Factors
2001
Structural biology. Actin' up.
De La Cruz E, Pollard T. Structural biology. Actin' up. Science 2001, 293: 616-8. PMID: 11474090, DOI: 10.1126/science.1063558.Peer-Reviewed Original ResearchActin Depolymerizing FactorsActinsAdenosine DiphosphateAdenosine TriphosphateBiopolymersContractile ProteinsCrystallography, X-RayHydrolysisMicrofilament ProteinsPhosphatesProfilinsProtein BindingProtein ConformationProtein Structure, SecondaryProtein Structure, TertiaryProtein SubunitsRhodaminesThymosinKinetic Mechanism and Regulation of Myosin VI*
De La Cruz E, Ostap E, Sweeney H. Kinetic Mechanism and Regulation of Myosin VI*. Journal Of Biological Chemistry 2001, 276: 32373-32381. PMID: 11423557, DOI: 10.1074/jbc.m104136200.Peer-Reviewed Original ResearchConceptsHeavy chain phosphorylationMyosin VIPhysiological nucleotide concentrationsADP releaseHigh duty ratio motorMolecular basisUnique adaptationsActin filamentsATP bindsATPase cycleNative dimerRate-limiting stepDetailed kinetic analysisChain phosphorylationRegulationNucleotide concentrationsDiffusional encounterMyosinLow affinityMutantsProcessivityKinetic analysisPhosphorylationActinBinds
2000
Actin and Light Chain Isoform Dependence of Myosin V Kinetics †
De La Cruz E, Wells A, Sweeney H, Ostap E. Actin and Light Chain Isoform Dependence of Myosin V Kinetics †. Biochemistry 2000, 39: 14196-14202. PMID: 11087368, DOI: 10.1021/bi001701b.Peer-Reviewed Original ResearchADP Inhibition of Myosin V ATPase Activity
De La Cruz E, Sweeney H, Ostap E. ADP Inhibition of Myosin V ATPase Activity. Biophysical Journal 2000, 79: 1524-1529. PMID: 10969013, PMCID: PMC1301045, DOI: 10.1016/s0006-3495(00)76403-4.Peer-Reviewed Original ResearchPolymerization and structure of nucleotide-free actin filaments11Edited by W. Baumeister
De La Cruz E, Mandinova A, Steinmetz M, Stoffler D, Aebi U, Pollard T. Polymerization and structure of nucleotide-free actin filaments11Edited by W. Baumeister. Journal Of Molecular Biology 2000, 295: 517-526. PMID: 10623543, DOI: 10.1006/jmbi.1999.3390.Peer-Reviewed Original Research