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
Avoiding 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
2011
Structural 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
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