2024
High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations
Xu X, Cao W, Swift M, Pandit N, Huehn A, Sindelar C, De La Cruz E, Hanein D, Volkmann N. High-resolution yeast actin structures indicate the molecular mechanism of actin filament stiffening by cations. Communications Chemistry 2024, 7: 164. PMID: 39079963, PMCID: PMC11289367, DOI: 10.1038/s42004-024-01243-x.Peer-Reviewed Original ResearchActin filamentsVertebrate actinsActin structuresDNase I binding loopActin filament assemblyEukaryotic cell functionStructures of wild-typeNear-atomic resolution structuresPotential binding sitesActin subunitsFilament assemblyRegulatory proteinsDNase IA167ActinAdjacent subunitsRegulatory roleMolecular mechanismsVertebratesWild-typeGlutamic acidCell functionFilamentsSubunitResiduesPublisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Publisher Correction: Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2354. PMID: 38491023, PMCID: PMC10943100, DOI: 10.1038/s41467-024-46804-9.Peer-Reviewed Original ResearchCryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex
Chavali S, Chou S, Cao W, Pollard T, De La Cruz E, Sindelar C. Cryo-EM structures reveal how phosphate release from Arp3 weakens actin filament branches formed by Arp2/3 complex. Nature Communications 2024, 15: 2059. PMID: 38448439, PMCID: PMC10918085, DOI: 10.1038/s41467-024-46179-x.Peer-Reviewed Original ResearchConceptsArp2/3 complexActin filamentsCryo-EM structureMother filamentDaughter filamentArp2/3 complex nucleates branched actin filamentsActin filament branchingBranched actin filamentsDissociation of PiADP-PiFilament branchingOrganelle movementADP stateBranch junctionsArp3A-resolutionActinArp2/3ADP-BeFxFilamentsADPPhosphate releaseFilament mechanismArp2Organelles
2018
The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments
Huehn A, Cao W, Elam WA, Liu X, De La Cruz EM, Sindelar CV. The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments. Journal Of Biological Chemistry 2018, 293: 5377-5383. PMID: 29463680, PMCID: PMC5900768, DOI: 10.1074/jbc.ac118.001843.Peer-Reviewed Original ResearchConceptsCofilin-decorated segmentsConformational changesCofilin/ADF proteinsActin-remodeling proteinsBind actin filamentsActin filament interactionsCofilin-induced changesEffects of cofilinCooperative conformational changesProtein occupancyADF proteinsCellular processesCell divisionStructure-based methodsCryo-EMActin segmentsIntracellular transportActin filamentsFilament twistCooperative bindingCofilinTwist changesActinFluorophore labelingSubunitsHigh-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing
Mentes A, Huehn A, Liu X, Zwolak A, Dominguez R, Shuman H, Ostap EM, Sindelar CV. High-resolution cryo-EM structures of actin-bound myosin states reveal the mechanism of myosin force sensing. Proceedings Of The National Academy Of Sciences Of The United States Of America 2018, 115: 1292-1297. PMID: 29358376, PMCID: PMC5819444, DOI: 10.1073/pnas.1718316115.Peer-Reviewed Original ResearchConceptsN-terminal subdomainHigh-resolution cryo-EM structuresADP stateNear-atomic resolution structuresCryo-EM structureCryo-electron microscopyHigh-resolution structuresIsoform-dependent mannerFilamentous actinResolution structureStructural basisMyosin IBActin filamentsStructural diversityRelease pathwayADP releaseActinPointed endPotent stabilizerMyosin