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
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 Research
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 rolesEndocytosisProteinClathrinStructural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex
Ti SC, Jurgenson CT, Nolen BJ, Pollard TD. Structural and biochemical characterization of two binding sites for nucleation-promoting factor WASp-VCA on Arp2/3 complex. Proceedings Of The National Academy Of Sciences Of The United States Of America 2011, 108: e463-e471. PMID: 21676862, PMCID: PMC3158158, DOI: 10.1073/pnas.1100125108.Peer-Reviewed Original Research