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 functionFilamentsSubunitResidues
2016
Cations 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
2008
Effects 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 ResearchConceptsADP-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
2004
Cofilin Binding to Muscle and Non-muscle Actin Filaments: Isoform-dependent Cooperative Interactions
De La Cruz EM. Cofilin Binding to Muscle and Non-muscle Actin Filaments: Isoform-dependent Cooperative Interactions. Journal Of Molecular Biology 2004, 346: 557-564. PMID: 15670604, DOI: 10.1016/j.jmb.2004.11.065.Peer-Reviewed Original ResearchConceptsActin filamentsConcentration of cofilinActin isoformsFilament severingRegulatory proteinsCooperative free energyActin fluorescencePyrene-actin fluorescenceCofilinFilament bindingHuman cofilinEquilibrium bindingCooperative interactionsIntrinsic affinitySkeletal muscleIsoformsBindingFilamentsSeveringMuscle actinHill coefficientCooperativity modelFilament latticeIsolated siteProtein