2024
Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail
Sexton J, Potchernikov T, Bibeau J, Casanova-Sepúlveda G, Cao W, Lou H, Boggon T, De La Cruz E, Turk B. Distinct functional constraints driving conservation of the cofilin N-terminal regulatory tail. Nature Communications 2024, 15: 1426. PMID: 38365893, PMCID: PMC10873347, DOI: 10.1038/s41467-024-45878-9.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActin Depolymerizing FactorsActinsCofilin 1HumansLim KinasesPhosphorylationSaccharomyces cerevisiaeConceptsN-terminal regionActin bindingSequence requirementsLIM kinaseAnalysis of individual variantsInactivates cofilinS. cerevisiaeRegulatory tailFamily proteinsActin depolymerizationPhosphorylation sitesKinase recognitionSequence variantsInhibitory phosphorylationCofilinN-terminusIndividual variantsFunctional constraintsActinDisordered sequencesPhosphorylationSequenceBiochemical analysisSequence constraintsKinase
2022
The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release
Gray S, Cao W, Montpetit B, De La Cruz EM. The nucleoporin Gle1 activates DEAD-box protein 5 (Dbp5) by promoting ATP binding and accelerating rate limiting phosphate release. Nucleic Acids Research 2022, 50: 3998-4011. PMID: 35286399, PMCID: PMC9023272, DOI: 10.1093/nar/gkac164.Peer-Reviewed Original ResearchConceptsNuclear pore complexRNA exportDEAD-box protein Dbp5ATPase cycleDbp5's ATPase activityDEAD (Asp-Glu-Ala-Asp) box protein 5Pore complexDbp5ATP bindingATPase cyclingNucleotide stateCytoplasmic faceGle1Pool of ATPADP-PiGene expressionProtein 5Mechanistic understandingNucleoporinsNup159ATPase activityATP dissociationATPPi releasePi release rate
2015
Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5)
Wong EV, Cao W, Vörös J, Merchant M, Modis Y, Hackney DD, Montpetit B, De La Cruz EM. Pi Release Limits the Intrinsic and RNA-Stimulated ATPase Cycles of DEAD-Box Protein 5 (Dbp5). Journal Of Molecular Biology 2015, 428: 492-508. PMID: 26730886, PMCID: PMC4744555, DOI: 10.1016/j.jmb.2015.12.018.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesDEAD-box RNA HelicasesKineticsNucleocytoplasmic Transport ProteinsPhosphatesRNASaccharomyces cerevisiaeSaccharomyces cerevisiae Proteins
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 ResearchMeSH KeywordsActin CytoskeletonCationsCell MovementChromatography, AffinityCofilin 1Cryoelectron MicroscopyHumansModels, MolecularSaccharomyces cerevisiaeConceptsFilament 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
2011
Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing
McCullough BR, Grintsevich EE, Chen CK, Kang H, Hutchison AL, Henn A, Cao W, Suarez C, Martiel JL, Blanchoin L, Reisler E, De La Cruz EM. Cofilin-Linked Changes in Actin Filament Flexibility Promote Severing. Biophysical Journal 2011, 101: 151-159. PMID: 21723825, PMCID: PMC3127193, DOI: 10.1016/j.bpj.2011.05.049.Peer-Reviewed Original ResearchMechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins
Cao W, Coman MM, Ding S, Henn A, Middleton ER, Bradley MJ, Rhoades E, Hackney DD, Pyle AM, De La Cruz EM. Mechanism of Mss116 ATPase Reveals Functional Diversity of DEAD-Box Proteins. Journal Of Molecular Biology 2011, 409: 399-414. PMID: 21501623, PMCID: PMC3125984, DOI: 10.1016/j.jmb.2011.04.004.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine DiphosphateAdenosine TriphosphatasesDEAD-box RNA HelicasesIntronsRNASaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsThermodynamicsConceptsGroup II intronsWeak RNARNA bindingDEAD-box RNA helicase proteinATP hydrolysisBiochemical intermediatesDEAD-box proteinsRNA helicase proteinStrong RNA bindingStable RNA duplexAbsence of nucleotideATP utilizationStrong thermodynamic couplingFunctional diversityIntron splicingStrong RNAIntron foldingVivo splicingHelicase proteinMRNA translationMss116ATPase cyclingVivo functionBiological roleADP state