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
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
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 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 toolPatches
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
Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex
Nolen BJ, Pollard TD. Insights into the Influence of Nucleotides on Actin Family Proteins from Seven Structures of Arp2/3 Complex. Molecular Cell 2007, 26: 449-457. PMID: 17499050, PMCID: PMC1997283, DOI: 10.1016/j.molcel.2007.04.017.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAdenosine DiphosphateAdenosine TriphosphatasesAdenosine TriphosphateAnimalsBinding SitesCattleCross-Linking ReagentsGlutaralHumansKineticsMacromolecular SubstancesModels, MolecularNucleotidesProtein ConformationProtein Interaction MappingProtein Structure, TertiaryConceptsArp2/3 complexATP bindingSubdomain 1Actin-family proteinsConformational changesLarge-scale conformational changesActin filament branchesNetwork of interactionsInfluence of nucleotidesActin familyFamily proteinsActin structuresFilament branchesIntrinsic disorderArp3ATPase cycleSteric clashesArp2/3Arp2NucleotidesResiduesComplexesBindingAdenine nucleotidesNew electron density
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
2003
Spatial and Temporal Pathway for Assembly and Constriction of the Contractile Ring in Fission Yeast Cytokinesis
Wu JQ, Kuhn JR, Kovar DR, Pollard TD. Spatial and Temporal Pathway for Assembly and Constriction of the Contractile Ring in Fission Yeast Cytokinesis. Developmental Cell 2003, 5: 723-734. PMID: 14602073, DOI: 10.1016/s1534-5807(03)00324-1.Peer-Reviewed Original Research