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 eventD179Cryo-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 mechanismArp2Organelles
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
2019
Mechanism 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
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 rateGenesMutationsCellsFilaments
2013
Actin Filament Severing by Cofilin Dismantles Actin Patches and Produces Mother Filaments for New Patches
Chen Q, Pollard TD. Actin Filament Severing by Cofilin Dismantles Actin Patches and Produces Mother Filaments for New Patches. Current Biology 2013, 23: 1154-1162. PMID: 23727096, PMCID: PMC4131202, DOI: 10.1016/j.cub.2013.05.005.Peer-Reviewed Original ResearchConceptsSites of endocytosisActin patchesWild-type cellsArp2/3 complexMother filamentActin filamentsAdaptor proteinActin polymerizationYeast cellsBranched actin filament networksEndocytic adaptor proteinActivators of Arp2/3Fission yeast cellsActin filament severingActin filament networkNew patchesEndocytic sitesQuantitative fluorescence microscopyMutant cofilinsMutant cellsNascent sitesFilament severingCofilinFilament networkEndocytosis
2011
Distinct Roles for F-BAR Proteins Cdc15p and Bzz1p in Actin Polymerization at Sites of Endocytosis in Fission Yeast
Arasada R, Pollard TD. Distinct Roles for F-BAR Proteins Cdc15p and Bzz1p in Actin Polymerization at Sites of Endocytosis in Fission Yeast. Current Biology 2011, 21: 1450-1459. PMID: 21885283, PMCID: PMC3350781, DOI: 10.1016/j.cub.2011.07.046.Peer-Reviewed Original ResearchConceptsF-BAR proteinsNucleation-promoting factorsActin patchesFission yeastArp2/3 complexActin polymerizationActin filamentsGenetic interaction experimentsSites of endocytosisPeripheral membrane proteinsActin binding proteinsClathrin-mediated endocytosisMembrane scissionYeast showSH3 domainCdc15pMembrane proteinsMembrane tubulesPlasma membraneGenetic analysisBinding proteinDistinct rolesEndocytosisProteinClathrin
2007
Assembly Mechanism of the Contractile Ring for Cytokinesis by Fission Yeast
Vavylonis D, Wu JQ, Hao S, O'Shaughnessy B, Pollard TD. Assembly Mechanism of the Contractile Ring for Cytokinesis by Fission Yeast. Science 2007, 319: 97-100. PMID: 18079366, DOI: 10.1126/science.1151086.Peer-Reviewed Original ResearchConceptsContractile ringActin filamentsLive fission yeast cellsIndividual daughter cellsFission yeast cellsDynamic actin filamentsFission yeastMotor protein myosinCell equatorDaughter cellsYeast cellsAssembly mechanismProtein myosinFluorescence microscopyCytokinesisMyosinFilamentsTransient connectionsCellsYeastFungiMechanismMeshwork
2006
Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin
Kovar DR, Harris ES, Mahaffy R, Higgs HN, Pollard TD. Control of the Assembly of ATP- and ADP-Actin by Formins and Profilin. Cell 2006, 124: 423-435. PMID: 16439214, DOI: 10.1016/j.cell.2005.11.038.Peer-Reviewed Original ResearchConceptsATP hydrolysisTotal internal reflection fluorescence microscopyActin filament polymerizationReflection fluorescence microscopyDiversity of functionsPresence of profilinMammalian forminFormin proteinsFormin mDia1Processive elongationFilament polymerizationForminsActin filamentsBiochemical activityBarbed endsProfilinFluorescence microscopyADP-actinAssembly stepsRecent studiesMDia1Common featureProcessivityElongationProtein