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 ResearchMeSH KeywordsActin CytoskeletonActinsAdenosine TriphosphateCryoelectron MicroscopyHydrogen BondingMagnesiumMolecular Dynamics SimulationPhosphatesConceptsCryo-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 eventD179
2018
Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments
Espinoza-Sanchez S, Metskas LA, Chou SZ, Rhoades E, Pollard TD. Conformational changes in Arp2/3 complex induced by ATP, WASp-VCA, and actin filaments. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: e8642-e8651. PMID: 30150414, PMCID: PMC6140485, DOI: 10.1073/pnas.1717594115.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