2024
High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations
Xu X, Cao W, Swift M, Pandit N, Huehn A, Sindelar C, De La Cruz E, Hanein D, Volkmann N. High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations. Communications Chemistry 2024, 7: 164. PMID: 39079963, PMCID: PMC11289367, DOI: 10.1038/s42004-024-01243-x.Peer-Reviewed Original ResearchActin filamentsVertebrate actinsActin structuresDNase I binding loopActin filament assemblyEukaryotic cell functionStructures of wild-typeNear-atomic resolution structuresPotential binding sitesActin subunitsFilament assemblyRegulatory proteinsDNase IA167ActinAdjacent subunitsRegulatory roleMolecular mechanismsVertebratesWild-typeGlutamic acidCell functionFilamentsSubunitResiduesPublisher Correction: 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. Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2354. PMID: 38491023, PMCID: PMC10943100, DOI: 10.1038/s41467-024-46804-9.Peer-Reviewed Original ResearchCryo-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 ResearchConceptsArp2/3 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 mechanismArp2OrganellesToxoplasma gondii actin filaments are tuned for rapid disassembly and turnover
Hvorecny K, Sladewski T, De La Cruz E, Kollman J, Heaslip A. Toxoplasma gondii actin filaments are tuned for rapid disassembly and turnover. Nature Communications 2024, 15: 1840. PMID: 38418447, PMCID: PMC10902351, DOI: 10.1038/s41467-024-46111-3.Peer-Reviewed Original ResearchConceptsActin filamentsDynamic properties of actin filamentsProperties of actin filamentsCytoskeletal protein actinFilamentous actin networkSkeletal muscle actinCryo-EM structureIn vitro assemblyOrganelle inheritanceD-loopActin networkNucleotide exchangeLive cell imagingProteins actinSkeletal actinConserved structureEvolutionary changesActinApicomplexan parasitesAssembly contactsIntracellular parasitesMonomer dissociationApicomplexanFilamentsBiophysical propertiesDistinct 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 ResearchConceptsN-terminal regionActin bindingSequence requirementsLIM kinaseAnalysis of individual variantsInactivates cofilinS. cerevisiaeRegulatory tailFamily proteinsActin depolymerizationPhosphorylation sitesKinase recognitionSequence variantsInhibitory phosphorylationCofilinN-terminusIndividual variantsFunctional constraintsActinDisordered sequencesPhosphorylationSequenceBiochemical analysisSequence constraintsKinase
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
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 modulationActinRegulation
2008
The Roles of Thymosin β4 in Cell Migration and Cell-to-Cell Signaling in Disease
Au J, Krendel M, Safer D, De La Cruz E. The Roles of Thymosin β4 in Cell Migration and Cell-to-Cell Signaling in Disease. Protein Reviews 2008, 218-228. DOI: 10.1007/978-0-387-71749-4_9.Peer-Reviewed Original ResearchΒ-thymosinsMetazoan cellsExtracellular cuesCell signalingFree actin monomersFilament elongationMonomeric actinActin monomersCell migrationInduction of angiogenesisRegulatory effectsTumor metastasisThymosin β4CellsTherapeutic applicationsSignalingPolypeptideActinΒ4High concentrationsAngiogenesisInductionFamilyComplexesTβ4Overview: Actin-Binding Protein Function and Its Relation to Disease Pathology
Krendel M, De La Cruz E. Overview: Actin-Binding Protein Function and Its Relation to Disease Pathology. Protein Reviews 2008, 65-82. DOI: 10.1007/978-0-387-71749-4_5.Peer-Reviewed Original ResearchFundamental cellular processesForm of ATPHydrolysis of ATPActin cytoskeletonProtein functionCellular processesMyosin familyMotor proteinsActin filamentsActin monomersATP moleculesCell membraneDistinct mechanismsPathogenic bacteriaGenerate movementDisease pathologyATPFilamentsForce generationMotilityCytoskeletonOrganellesChemical energyProteinActin
2001
Kinetic 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 analysisPhosphorylationActinBindsActin-Binding Proteins: An Overview
De La Cruz E. Actin-Binding Proteins: An Overview. Results And Problems In Cell Differentiation 2001, 32: 123-134. PMID: 11131827, DOI: 10.1007/978-3-540-46560-7_9.Peer-Reviewed Original Research
2000
Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers
De La Cruz E, Ostap E, Brundage R, Reddy K, Sweeney H, Safer D. Thymosin-β4 Changes the Conformation and Dynamics of Actin Monomers. Biophysical Journal 2000, 78: 2516-2527. PMID: 10777749, PMCID: PMC1300842, DOI: 10.1016/s0006-3495(00)76797-x.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsBinding SitesBiophysical PhenomenaBiophysicsCircular DichroismCross-Linking ReagentsFluorescent DyesHumansIn Vitro TechniquesKineticsMacromolecular SubstancesModels, MolecularMuscle, SkeletalMutagenesis, Site-DirectedNaphthalenesulfonatesOsmotic PressureProtein BindingProtein ConformationRabbitsRecombinant ProteinsThermodynamicsThymosinTritiumViscosityConceptsActin monomersActin monomer poolMgATP-actinMetazoan cellsNucleotide exchangeC-terminusSubdomain 2Conformational changesMonomer poolN-iodoacetyl-N'Cleavage siteActinThymosin β4Rate of dissociationAmide protonsSulfo-1Unique abilityBindingStructural dynamicsConformationTerminusNucleotidesProteolysisDifferent stabilitiesDegrees C
1998
Regulation of G protein-coupled Receptor Kinase 5 (GRK5) by Actin*
Freeman J, De La Cruz E, Pollard T, Lefkowitz R, Pitcher J. Regulation of G protein-coupled Receptor Kinase 5 (GRK5) by Actin*. Journal Of Biological Chemistry 1998, 273: 20653-20657. PMID: 9685424, DOI: 10.1074/jbc.273.32.20653.Peer-Reviewed Original ResearchConceptsG protein-coupled receptor kinase 5G protein-coupled receptorsG protein-coupled receptor kinasesAgonist-occupied G protein-coupled receptorsAmino terminusPhosphorylation of GPCRsSoluble substratesMembrane-bound substratesProtein-coupled receptor kinasesMembrane-bound G protein-coupled receptorReceptor kinase 5Receptor kinasePresence of actinSubstrate specificityKinase activityActin filamentsActin bindsKinase 5Actin monomersAmino acidsPhosphorylationActinCalmodulinTerminusKinaseInteractions of Acanthamoeba Profilin with Actin and Nucleotides Bound to Actin †
Vinson V, De La Cruz E, Higgs H, Pollard T. Interactions of Acanthamoeba Profilin with Actin and Nucleotides Bound to Actin †. Biochemistry 1998, 37: 10871-10880. PMID: 9692980, DOI: 10.1021/bi980093l.Peer-Reviewed Original ResearchConceptsMg-ATPAcanthamoeba profilinMg-ADPExchange of ADPRabbit skeletal muscle actinAffinity of profilinSkeletal muscle actinFree barbed endsProfilin bindingSerine 38Nucleotide exchangeBarbed endsCysteine 374Actin monomersProfilinMuscle actinActinUnique siteIntrinsic fluorescenceFluorescence anisotropyATP-actinSubunit/Free actinSame affinityATP