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
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