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 tools
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 organizationProtein
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
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