2025
Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer
Iyer S, Wu J, Pollard T, Voth G. Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2421467122. PMID: 40048273, PMCID: PMC11912402, DOI: 10.1073/pnas.2421467122.Peer-Reviewed Original ResearchConceptsArp2/3 complexActin monomersNeuronal Wiskott-Aldrich syndrome proteinWiskott-Aldrich syndrome proteinActin filament branchingMammalian Arp2/3 complexArp2/3 complex activationNucleation-promoting factorsActin-related proteinsCA motifsD-loopActin filamentsFilament branchingOrganelle movementBranch formationActive conformationActinMolecular mechanismsArp2/3Binding sitesArp3ProteinPathwayAtomistic molecular dynamics simulationsComplex activityFast Actin Disassembly and Fimbrin Mechanosensitivity Support Rapid Turnover in a Model of Clathrin‐Mediated Endocytosis
Mousavi S, Lacy M, Li X, Berro J. Fast Actin Disassembly and Fimbrin Mechanosensitivity Support Rapid Turnover in a Model of Clathrin‐Mediated Endocytosis. Cytoskeleton 2025 PMID: 40035221, DOI: 10.1002/cm.22002.Peer-Reviewed Original ResearchClathrin-mediated endocytosisActin filament disassemblyDynamics of actinActin-interacting proteinHigh membrane tensionActin meshworkEndocytic proteinsFilament disassemblyActin disassemblyNascent filamentsActin cytoskeletonEndocytic structuresEukaryotic cellsBinding partnersCellular processesTurgor pressureFimbrinActinRapid turnoverMembrane tensionEndocytosisProteinFilamentsDisassemblyYeastHigh-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory
Chavali S, Carman P, Shuman H, Ostap E, Sindelar C. High-resolution structures of Myosin-IC reveal a unique actin-binding orientation, ADP release pathway, and power stroke trajectory. Proceedings Of The National Academy Of Sciences Of The United States Of America 2025, 122: e2415457122. PMID: 40014570, PMCID: PMC11892617, DOI: 10.1073/pnas.2415457122.Peer-Reviewed Original ResearchConceptsN-terminal extensionATP bindingRegulating ATP bindingADP releaseClass I myosinsLever arm swingStructure of myosinCryo-EM structureHigh-resolution structuresMembrane-bound vesiclesActin interfaceMyosin superfamilyMyosin familyActin filamentsAbsence of ADPMembrane remodelingNucleotide pocketMotile behaviorMyo1cPlasma membraneBiological functionsActinCryo-EM dataMotor domainMyosin
2024
Bending stiffness of Toxoplasma gondii actin filaments
Cao W, Sladewski T, Heaslip A, De La Cruz E. Bending stiffness of Toxoplasma gondii actin filaments. Journal Of Biological Chemistry 2024, 301: 108101. PMID: 39706262, PMCID: PMC11786770, DOI: 10.1016/j.jbc.2024.108101.Peer-Reviewed Original ResearchConceptsActin filamentsD-loopMechanical properties of actin filamentsFilament subunitsSkeletal muscle actin filamentsProperties of actin filamentsSkeletal muscle actinMuscle actin filamentsFilament length distributionApicomplexan parasite Toxoplasma gondiiIntersubunit salt bridgesOrganelle inheritancePointed-endSubunit interactionsNeighboring subunitUnique assembly propertiesSalt bridgesSubunitFunctional consequencesSubunit dissociationVisible densityActinSubunit incorporationParasite Toxoplasma gondiiFilamentsEctopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation
Falahati H, Wu Y, Fang M, De Camilli P. Ectopic reconstitution of a spine-apparatus-like structure provides insight into mechanisms underlying its formation. Current Biology 2024, 35: 265-276.e4. PMID: 39626668, PMCID: PMC11753949, DOI: 10.1016/j.cub.2024.11.010.Peer-Reviewed Original ResearchEndoplasmic reticulumSpine apparatusActin bundlesEndomembrane networkER sheetsConserved regionProtein synaptopodinCisternal organelleNon-neuronal cellsER cisternsOrganellesSynaptopodinProteinNeuronal dendritesNeuronal spinesAxon initial segmentFindings shed lightBiogenesisActinProtein matrixNarrow lumenReticulumMammalsInitial segmentMechanismSubstrate geometry and topography induce F-actin reorganization and chiral alignment in an adherent model cortex
Sakamoto R, Murrell M. Substrate geometry and topography induce F-actin reorganization and chiral alignment in an adherent model cortex. Cell Reports Physical Science 2024, 5: 102338. DOI: 10.1016/j.xcrp.2024.102338.Peer-Reviewed Original ResearchF-actin organizationF-actin networkF-actinF-actin reorganizationSubstrate featuresActin cortexCytoskeletal organizationGiant unilamellar vesiclesIntracellular signalingCell adhesionGeometry sensingLiposome shapeCell membraneMembrane deformationUnilamellar vesiclesAdherent liposomeCellsActinOrganizationVesiclesAdhesionLiposomesMechanical power is maximized during contractile ring-like formation in a biomimetic dividing cell model
Sakamoto R, Murrell M. Mechanical power is maximized during contractile ring-like formation in a biomimetic dividing cell model. Nature Communications 2024, 15: 9731. PMID: 39523366, PMCID: PMC11551154, DOI: 10.1038/s41467-024-53228-y.Peer-Reviewed Original ResearchConceptsMyosin-induced stressContractile ring assemblyCell division mechanismActin filamentsActin cortexCleavage furrowDivision planeActomyosin flowsGiant unilamellar vesiclesRing assemblyCell divisionMyosin activityContractile ring-like structureShape changesRing-like structureDivision mechanismEnergetic costSymmetric divisionActinRing-like formationCell modelUnilamellar vesiclesIn vitro modelFurrowCellsRegulation and signaling of the LIM domain kinases
Casanova‐Sepúlveda G, Boggon T. Regulation and signaling of the LIM domain kinases. BioEssays 2024, 47: e2400184. PMID: 39361252, PMCID: PMC11663136, DOI: 10.1002/bies.202400184.Peer-Reviewed Original ResearchLIM domain kinaseDownstream of Rho GTPasesCofilin/actin depolymerizing factorActin cytoskeleton regulationIntra-molecular mechanismFilament severingDepolymerizing factorRho GTPasesActin depolymerizationCytoskeleton regulationRegulation mechanismKinaseLIMProteinRegulationGTPaseLIMK2LIMK1ActinEnzymeHuman healthSignalDepolymerizationCascadeMechanismCross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis
Ren Y, Yang J, Fujita B, Zhang Y, Berro J. Cross-regulations of two connected domains form a mechanical circuit for steady force transmission during clathrin-mediated endocytosis. Cell Reports 2024, 43: 114725. PMID: 39276354, PMCID: PMC11476202, DOI: 10.1016/j.celrep.2024.114725.Peer-Reviewed Original ResearchClathrin-mediated endocytosisF-actinActin cytoskeletonFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeCell adhesion complexAdhesion complexesMembrane localizationPN forcesStable bindingEnd4pCross-regulationCytoskeletonActinEndocytosisMembraneBindingMechanical forcesTalinTransmission of forcesThatchForce transmissionDomainCellsFissionEnergy partitioning in the cell cortex
Chen S, Seara D, Michaud A, Kim S, Bement W, Murrell M. Energy partitioning in the cell cortex. Nature Physics 2024, 20: 1824-1832. DOI: 10.1038/s41567-024-02626-6.Peer-Reviewed Original ResearchCell cortexEntropy production rateGAP expressionCortical actin filamentsRho GTPase pathwayGTPase pathwayMyosin IIActin filamentsDiversity patternsEnergy partitioningRhoOnsager reciprocityCell phenotypeProtein expressionThermodynamic equilibriumCellsSpiral travelling waveProduction rateTemporal dynamicsLiving systemsActinEnergyWavePhenotypeActivityHigh-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 functionFilamentsSubunitResiduesComposite branched and linear F-actin maximize myosin-induced membrane shape changes in a biomimetic cell model
Sakamoto R, Murrell M. Composite branched and linear F-actin maximize myosin-induced membrane shape changes in a biomimetic cell model. Communications Biology 2024, 7: 840. PMID: 38987288, PMCID: PMC11236970, DOI: 10.1038/s42003-024-06528-4.Peer-Reviewed Original ResearchConceptsF-actin networkF-actinF-actin architectureMembrane shape changesCell shape changesActivity of myosinInduce membrane deformationActomyosin contractilityShape changesActin cortexActomyosin cortexGiant unilamellar vesiclesActinMembrane deformationUnilamellar vesiclesCell modelNo-slip boundariesForce generationActomyosinMyosinVesiclesForce transmissionCompetition and synergy of Arp2/3 and formins in nucleating actin waves
Le Chua X, San Tong C, Su M, Xǔ X, Xiao S, Wu X, Wu M. Competition and synergy of Arp2/3 and formins in nucleating actin waves. Cell Reports 2024, 43: 114423. PMID: 38968072, PMCID: PMC11378572, DOI: 10.1016/j.celrep.2024.114423.Peer-Reviewed Original ResearchActin wavesActin regulatory proteinsActin cytoskeletal networkConstitutively active mutantArp2/3 complexActin assemblyMonomeric actinActive Cdc42Cdc42-interactingCytoskeletal networkArp2/3Active mutantCellular processesRegulatory proteinsUpstream regulatorCdc42ActinPlasma membraneFMNL1Complex feedback loopsForminPhysiological stateDelayed recruitmentFeedback loopGTPaseActive tension and membrane friction mediate cortical flows and blebbing in a model actomyosin cortex
Sakamoto R, Murrell M. Active tension and membrane friction mediate cortical flows and blebbing in a model actomyosin cortex. Physical Review Research 2024, 6: 033024. DOI: 10.1103/physrevresearch.6.033024.Peer-Reviewed Original ResearchActomyosin cortexCell membraneActin cytoskeletonCortical flowMembrane blebbingCell divisionCell migrationCytoskeletonActomyosinBiological phenomenaMembrane bulgesBlebsCellsMembraneViscoelastic fluidMechanical responseElastic stressesStress yieldActinUbiquitous structuresApoptosisMechanical stressMembrane elasticityPhysical behaviorGrowth‐induced collective bending and kinetic trapping of cytoskeletal filaments
Banerjee D, Freedman S, Murrell M, Banerjee S. Growth‐induced collective bending and kinetic trapping of cytoskeletal filaments. Cytoskeleton 2024, 81: 409-419. PMID: 38775207, DOI: 10.1002/cm.21877.Peer-Reviewed Original ResearchActin networkFilamentous growthActin filamentsTurnover of actin filamentsActin filament growthKinetic trapsActin poolFilament polymerizationActin cortexCytoskeletal filamentsSubunit poolActinFilamentsSubunitConsequence of growthFilament mechanismNematic defectsCrowded environmentLong-livedGrowthPoolAbundanceBending patternCellsTurnoverF-actin architecture determines the conversion of chemical energy into mechanical work
Sakamoto R, Murrell M. F-actin architecture determines the conversion of chemical energy into mechanical work. Nature Communications 2024, 15: 3444. PMID: 38658549, PMCID: PMC11043346, DOI: 10.1038/s41467-024-47593-x.Peer-Reviewed Original ResearchConceptsF-actin architectureF-actinATP consumption rateF-actin bundlesIn vitro reconstitutionDynamic cellular processesHigher ATP consumptionActin cytoskeletonFilamentous actinMyosin motorsCellular processesATP hydrolysisPurified componentsAdenosine triphosphateForce generationConversion of chemical energyATP consumptionConsumption rateActinChemical energyMyosinNetwork contractionCytoskeletonEnergetic principlesHydrolysisCollective dynamics of actin and microtubule and its crosstalk mediated by FHDC1
San Tong C, Su M, Sun H, Le Chua X, Xiong D, Guo S, Raj R, Ong N, Lee A, Miao Y, Wu M. Collective dynamics of actin and microtubule and its crosstalk mediated by FHDC1. Frontiers In Cell And Developmental Biology 2024, 11: 1261117. PMID: 38567385, PMCID: PMC10985548, DOI: 10.3389/fcell.2023.1261117.Peer-Reviewed Original ResearchActin wavesActin polymerizationFormin-mediated actin polymerizationDynamics of actinMultiple cellular processesActin nucleationCell cortexCytoskeletal networkCellular processesMicrotubule networkCell divisionMicrotubule depolymerizationActinAntagonistic interplayMicrotubulesMolecular insightsProtein 1CellsCdc42Mast cellsConcurrent releaseDepolymerizationInteractionInhibitionPublisher 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 properties
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