2024
Mechanism of phosphate release from actin filaments
Wang Y, Wu J, Zsolnay V, Pollard T, Voth G. Mechanism of phosphate release from actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2408156121. PMID: 38980907, PMCID: PMC11260136, DOI: 10.1073/pnas.2408156121.Peer-Reviewed Original ResearchConceptsCryo-EM structureAll-atom molecular dynamics simulationsATP-actinRate of phosphate releaseActin filamentsMechanism of phosphate releaseMolecular dynamics simulationsPhosphate releaseDissociation of phosphateR177Salt bridgesHydrogen bondsEnergy barrierDynamics simulationsComputational studyRelease of phosphateFilamentsRelease pathwayInternal cavityResiduesStudy residuesOccluding interactionsGatePrimary eventD179Publisher 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 mechanismArp2OrganellesFreezing alters the conformational ensemble of actin filaments in molecular dynamics simulations
Iyer S, Pollard T, Voth G. Freezing alters the conformational ensemble of actin filaments in molecular dynamics simulations. Biophysical Journal 2024, 123: 537a-538a. DOI: 10.1016/j.bpj.2023.11.3250.Peer-Reviewed Original Research
2023
Discovery of the first unconventional myosin: Acanthamoeba myosin-I
Pollard T, Korn E. Discovery of the first unconventional myosin: Acanthamoeba myosin-I. Frontiers In Physiology 2023, 14: 1324623. PMID: 38046947, PMCID: PMC10693453, DOI: 10.3389/fphys.2023.1324623.Peer-Reviewed Original ResearchUnconventional myosinActin filamentsMyosin heavy chain kinaseFirst unconventional myosinsEvolution of eukaryotesClass I MyosinHeavy chain kinaseNovel unconventional myosinPhylogenetic analysisSlime moldMembrane lipidsChain kinaseProteolytic fragmentsHeavy chainMuscle myosinMyosinCofactorEnzymeMg-ATPaseMg-ATPase activityEukaryotesFilamentsCrude enzymeKinaseActin
2021
Sample Preparation and Laser Intensities Affect mEos3.2 Photophysics in Live and Fixed Fission Yeast Cells
Sun M, Hu K, Bewersdorf J, Pollard T. Sample Preparation and Laser Intensities Affect mEos3.2 Photophysics in Live and Fixed Fission Yeast Cells. Biophysical Journal 2021, 120: 354a. DOI: 10.1016/j.bpj.2020.11.2197.Peer-Reviewed Original Research
2019
The Functionally Important N‑Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation
Chatterjee M, Pollard TD. The Functionally Important N‑Terminal Half of Fission Yeast Mid1p Anillin Is Intrinsically Disordered and Undergoes Phase Separation. Biochemistry 2019, 58: 3031-3041. PMID: 31243991, PMCID: PMC7336169, DOI: 10.1021/acs.biochem.9b00217.Peer-Reviewed Original ResearchConceptsN-terminal halfFission yeast Schizosaccharomyces pombeYeast Schizosaccharomyces pombeC-terminal halfFull-length proteinSchizosaccharomyces pombeStructure prediction toolsPH domainScaffold proteinInsect cellsAnimal cellsContractile ringMyosin IIOrganizing centerAnillinMid1pProteinHydrodynamic measurementsPombeCytokinesisUndergoes phase separationCellsFungalPrediction toolsMechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides
Chou SZ, Pollard TD. Mechanism of actin polymerization revealed by cryo-EM structures of actin filaments with three different bound nucleotides. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 4265-4274. PMID: 30760599, PMCID: PMC6410863, DOI: 10.1073/pnas.1807028115.Peer-Reviewed Original ResearchConceptsATP hydrolysisActin filamentsBarbed endsMultiple favorable interactionsCryo-electron microscopyNetwork of interactionsShort-pitch helixActin polymerizationC-terminusAdjacent subunitsSubdomain 2Conformational changesEM structuresBinding loopSubdomain 3SubunitsPhosphate dissociationPointed endRelease sitesFilamentsActive siteConformationADPBackbone conformationSide chains
2018
Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments
Espinoza-Sanchez S, Metskas LA, Chou SZ, Rhoades E, Pollard TD. Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e8642-e8651. PMID: 30150414, PMCID: PMC6140485, DOI: 10.1073/pnas.1717594115.Peer-Reviewed Original Research
2017
The Effect of Intermolecular Interactions in the Elongation Rates of Actin Filament by Formins
Aydin F, Courtemanche N, Pollard T, Voth G. The Effect of Intermolecular Interactions in the Elongation Rates of Actin Filament by Formins. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.783.13.Peer-Reviewed Original ResearchFission Yeast Contractile Ring Tension Increases ∼2-Fold Throughout Constriction and Regulates Septum Closure but does not Set the Constriction Rate
Thiyagarajan S, Chin H, Karatekin E, Pollard T, O'Shaughnessy B. Fission Yeast Contractile Ring Tension Increases ∼2-Fold Throughout Constriction and Regulates Septum Closure but does not Set the Constriction Rate. Biophysical Journal 2017, 112: 30a. DOI: 10.1016/j.bpj.2016.11.196.Peer-Reviewed Original ResearchRedefining the Role of the Arp2/3 Complex: Regulation of Morphology at the Leading Edge
Anderson K, Page C, Swift M, Suraneni P, Janssen M, Pollard T, Li R, Volkmann N, Hanein D. Redefining the Role of the Arp2/3 Complex: Regulation of Morphology at the Leading Edge. Biophysical Journal 2017, 112: 16a. DOI: 10.1016/j.bpj.2016.11.120.Peer-Reviewed Original Research
2016
Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast
Laplante C, Huang F, Tebbs IR, Bewersdorf J, Pollard TD. Molecular organization of cytokinesis nodes and contractile rings by super-resolution fluorescence microscopy of live fission yeast. Proceedings Of The National Academy Of Sciences Of The United States Of America 2016, 113: e5876-e5885. PMID: 27647921, PMCID: PMC5056082, DOI: 10.1073/pnas.1608252113.Peer-Reviewed Original ResearchConceptsFluorescence photoactivation localization microscopyContractile ringLive fission yeast cellsLive fission yeastFission yeast cellsCytokinetic contractile ringSuper-resolution fluorescence microscopyCytokinesis nodesPhotoactivation localization microscopyFission yeastFormin Cdc12pActin networkIQ motifPlasma membraneCytokinesisConstituent proteinsMyosin-II tailYeast cellsActin ringsActin strandsAssembly precursorsDiscrete structural unitsFluorescence microscopyMolecular organizationProteinAvoiding artefacts when counting polymerized actin in live cells with LifeAct fused to fluorescent proteins
Courtemanche N, Pollard TD, Chen Q. Avoiding artefacts when counting polymerized actin in live cells with LifeAct fused to fluorescent proteins. Nature Cell Biology 2016, 18: 676-683. PMID: 27159499, PMCID: PMC5509211, DOI: 10.1038/ncb3351.Peer-Reviewed Original ResearchIn Fission Yeast the Constriction Rate is not Set by the Cytokinetic Ring, but by the Septum Growth Machinery
Thiyagarajan S, Munteanu E, Arasada R, Pollard T, O'Shaughnessy B. In Fission Yeast the Constriction Rate is not Set by the Cytokinetic Ring, but by the Septum Growth Machinery. Biophysical Journal 2016, 110: 306a-307a. DOI: 10.1016/j.bpj.2015.11.1647.Peer-Reviewed Original Research
2015
Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring
Laplante C, Berro J, Karatekin E, Hernandez-Leyva A, Lee R, Pollard TD. Three Myosins Contribute Uniquely to the Assembly and Constriction of the Fission Yeast Cytokinetic Contractile Ring. Current Biology 2015, 25: 1955-1965. PMID: 26144970, PMCID: PMC4526439, DOI: 10.1016/j.cub.2015.06.018.Peer-Reviewed Original ResearchConceptsContractile ringActin filamentsHeavy chain geneMyosin IIContractile ring assemblyFission yeast cellsMyosin heavy chain geneCytokinetic contractile ringConventional myosin IICytokinetic nodesMyo2Myo51Myp2Ring assemblyYeast cellsMyosin functionCytokinesisDeletion mutationsComplete assemblyMyosin VConstriction rateGenesMutationsCellsFilamentsActin Filament Nucleation is Influenced by Electrostatic Interactions with the Bni1p Formin FH2 Domain
Baker J, Courtemanche N, Parton D, McCullagh M, Pollard T, Voth G. Actin Filament Nucleation is Influenced by Electrostatic Interactions with the Bni1p Formin FH2 Domain. Biophysical Journal 2015, 108: 508a. DOI: 10.1016/j.bpj.2014.11.2782.Peer-Reviewed Original Research
2014
Local and global analysis of endocytic patch dynamics in fission yeast using a new “temporal superresolution” realignment method
Berro J, Pollard TD. Local and global analysis of endocytic patch dynamics in fission yeast using a new “temporal superresolution” realignment method. Molecular Biology Of The Cell 2014, 25: 3501-3514. PMID: 25143395, PMCID: PMC4230612, DOI: 10.1091/mbc.e13-01-0004.Peer-Reviewed Original ResearchConceptsFission yeastEndocytic actin patchesWild-type cellsEndocytic patchesActin patchesQuantitative microscopyActin assemblyCellular processesVesicle movementEndocytic vesiclesInterphase cellsVesicle formationMolecular mechanismsPatch dynamicsYeastCell lengthGlobal analysisNumber of patchesMicroscopy moviesCellsClathrinEndocytosisNew toolValuable toolPatchesMechanism of Cytokinetic Contractile Ring Constriction in Fission Yeast
Stachowiak MR, Laplante C, Chin HF, Guirao B, Karatekin E, Pollard TD, O’Shaughnessy B. Mechanism of Cytokinetic Contractile Ring Constriction in Fission Yeast. Developmental Cell 2014, 29: 547-561. PMID: 24914559, PMCID: PMC4137230, DOI: 10.1016/j.devcel.2014.04.021.Peer-Reviewed Original ResearchCytokinetic nodes in fission yeast arise from two distinct types of nodes that merge during interphase
Akamatsu M, Berro J, Pu KM, Tebbs IR, Pollard TD. Cytokinetic nodes in fission yeast arise from two distinct types of nodes that merge during interphase. Journal Of Cell Biology 2014, 204: 977-988. PMID: 24637325, PMCID: PMC3998791, DOI: 10.1083/jcb.201307174.Peer-Reviewed Original Research