2014
Site-specific cation release drives actin filament severing by vertebrate cofilin
Kang H, Bradley MJ, Cao W, Zhou K, Grintsevich EE, Michelot A, Sindelar CV, Hochstrasser M, De La Cruz EM. Site-specific cation release drives actin filament severing by vertebrate cofilin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 17821-17826. PMID: 25468977, PMCID: PMC4273407, DOI: 10.1073/pnas.1413397111.Peer-Reviewed Original ResearchConceptsFilament severingActin filamentsActin filament severingKey regulatory functionsConcentration of endsActin filament fragmentationEukaryotic cellsCation-binding sitesProtein cofilinDeletion mutantsS. cerevisiaeSubunit exchangeFilament turnoverActin polymerizationEssential functionsSite-specific interactionsCofilinMolecular mechanismsAssembly dynamicsRegulatory functionsActin moleculesFilament fragmentationFilament structureSustained motilitySevering
2012
Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness
Kang H, Bradley MJ, McCullough BR, Pierre A, Grintsevich EE, Reisler E, De La Cruz EM. Identification of cation-binding sites on actin that drive polymerization and modulate bending stiffness. Proceedings Of The National Academy Of Sciences Of The United States Of America 2012, 109: 16923-16927. PMID: 23027950, PMCID: PMC3479481, DOI: 10.1073/pnas.1211078109.Peer-Reviewed Original ResearchConceptsCation-binding sitesActin assemblyEukaryotic biologyLong-pitch helixActin functionSalt-dependent effectsCell divisionCell motilityActin polymerizationFilament assemblyAdjacent subunitsIntracellular transportActin filamentsPhysiological salt concentrationsActin monomersCellular shapeNonspecific ionic strength effectsDiscrete sites
2010
Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11
Kucera K, Koblansky AA, Saunders LP, Frederick KB, De La Cruz EM, Ghosh S, Modis Y. Structure-Based Analysis of Toxoplasma gondii Profilin: A Parasite-Specific Motif Is Required for Recognition by Toll-Like Receptor 11. Journal Of Molecular Biology 2010, 403: 616-629. PMID: 20851125, PMCID: PMC2957522, DOI: 10.1016/j.jmb.2010.09.022.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid MotifsAmino Acid SequenceAnimalsBase SequenceCrystallography, X-RayDNA PrimersImmunity, InnateIn Vitro TechniquesMacrophages, PeritonealMiceMice, KnockoutModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedMutant ProteinsPlasmodium falciparumProfilinsProtein Structure, SecondaryProtozoan ProteinsRabbitsRecombinant ProteinsSaccharomyces cerevisiae ProteinsSequence Homology, Amino AcidSignal TransductionStatic ElectricityToll-Like ReceptorsToxoplasmaConceptsAcidic loopToll-like receptor 11Β-hairpinLong β-hairpinApicomplexan parasite Cryptosporidium parvumActin-binding surfaceFilament barbed endsStructure-based analysisYeast profilinGondii profilinProfilin mutantsGliding motilityParasite Cryptosporidium parvumT. gondii profilinNucleotide exchangeToxoplasma gondii profilinRabbit actinPlasmodium falciparum resultsActin polymerizationApicomplexan protozoaHomologous loopBarbed endsHost cellsIL-12 secretionInnate immune response
2008
Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability
Frederick KB, Sept D, De La Cruz EM. Effects of Solution Crowding on Actin Polymerization Reveal the Energetic Basis for Nucleotide-Dependent Filament Stability. Journal Of Molecular Biology 2008, 378: 540-550. PMID: 18374941, PMCID: PMC2424216, DOI: 10.1016/j.jmb.2008.02.022.Peer-Reviewed Original ResearchConceptsADP-actin filamentsFilament stabilityCell structure maintenanceFundamental cellular processesADP-actinADP-F-actinSolution crowdingCellular processesAllosteric regulatorsMolecular basisRegulatory proteinsActin polymerizationATP hydrolysisActin activityNucleotide hydrolysisFilament subunitsEnergetic basisIntracellular conditionsStructure maintenanceSubunit dissociationStability of ATPATPConcentration-dependent mannerStructural differencesForce generation