2021
Tissue-specific dynamic codon redefinition in Drosophila
Hudson AM, Szabo NL, Loughran G, Wills NM, Atkins JF, Cooley L. Tissue-specific dynamic codon redefinition in Drosophila. Proceedings Of The National Academy Of Sciences Of The United States Of America 2021, 118: e2012793118. PMID: 33500350, PMCID: PMC7865143, DOI: 10.1073/pnas.2012793118.Peer-Reviewed Original ResearchConceptsStop codonTranslational stop codon readthroughReadthrough efficiencyHuman tissue culture cellsStop codon readthroughTissue-specific regulationAdult central nervous system (CNS) tissueTissue culture cellsReadthrough productKelch proteinUbiquitin ligaseSingle geneAdult brainIndividual proteinsCodon readthroughReadthroughViral mRNAsC-terminalMalpighian tubulesCodonNeuronal proteinsCell typesAmino acidsCulture cellsDrosophila
2014
Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers
Burn KM, Shimada Y, Ayers K, Vemuganti S, Lu F, Hudson A, Cooley L. Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers. Developmental Biology 2014, 398: 206-217. PMID: 25481758, PMCID: PMC4340711, DOI: 10.1016/j.ydbio.2014.11.021.Peer-Reviewed Original ResearchConceptsDrosophila insulin-like peptidesEgg chambersStarvation responseBody organizationDrosophila egg chamberMotor protein dyneinNutrient-rich conditionsPoor nutrient availabilityInsulin-like peptidesProcessing bodiesDrosophila femalesGermline cellsP-bodiesNutrient availabilityDynein activityInsulin signalingProgeny survivalInsulin pathwayKinesin activityFollicle cellsMicrotubulesStarvationBovine insulinPotential mechanismsProtective response
2002
Dcas Is Required for importin-α3 Nuclear Export and Mechano-Sensory Organ Cell Fate Specification in Drosophila
Tekotte H, Berdnik D, Török T, Buszczak M, Jones LM, Cooley L, Knoblich JA, Davis I. Dcas Is Required for importin-α3 Nuclear Export and Mechano-Sensory Organ Cell Fate Specification in Drosophila. Developmental Biology 2002, 244: 396-406. PMID: 11944946, DOI: 10.1006/dbio.2002.0612.Peer-Reviewed Original ResearchMeSH KeywordsActive Transport, Cell NucleusAlpha KaryopherinsAnimalsApoptosisCellular Apoptosis Susceptibility ProteinDNA HelicasesDrosophila melanogasterDrosophila ProteinsEmbryo, NonmammalianGene Expression Regulation, DevelopmentalIn Situ HybridizationMechanoreceptorsMorphogenesisPhylogenyRNA, MessengerSense OrgansConceptsNuclear exportEmbryonic central nervous systemNuclear protein importCell fate specificationSpecific developmental phenotypesHuman genetic disordersProtein importDrosophila orthologImportin alphaFate specificationExport receptorCell identityDevelopmental phenotypesHypomorphic alleleEmbryonic cellsVivo functionNotch pathwayTissue specificityCytoplasmic distributionEpidermal cellsDifferent tissuesCharacteristics of mutationsGenetic disordersMutationsPhenotype
2000
Physical and genetic interaction of filamin with presenilin in Drosophila
Guo Y, Zhang S, Sokol N, Cooley L, Boulianne G. Physical and genetic interaction of filamin with presenilin in Drosophila. Journal Of Cell Science 2000, 113: 3499-3508. PMID: 10984440, DOI: 10.1242/jcs.113.19.3499.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAlzheimer DiseaseAmino Acid SequenceAnimalsBlotting, WesternCarrier ProteinsCloning, MolecularContractile ProteinsDrosophila melanogasterEmbryo, NonmammalianFemaleFilaminsGene Expression Regulation, DevelopmentalHumansInsect ProteinsLarvaMaleMembrane ProteinsMicrofilament ProteinsMolecular Sequence DataPresenilin-1Presenilin-2Protein BindingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTwo-Hybrid System TechniquesConceptsN-terminal actin-binding domainOverall amino acid identityOverexpression of presenilinFamilial Alzheimer's diseaseTransmembrane domain proteinActin-binding domainAmino acid identityLarge hydrophilic loopDrosophila filaminDomain proteinsGenetic interactionsAlternative splicingHydrophilic loopAcid identityTerminal domainDrosophilaHuman filaminChromosome 3Spliced formsFilaminAdult phenotypeLoop regionPresenilinNovel familyLong form
1997
Examination of the function of two kelch proteins generated by stop codon suppression
Robinson D, Cooley L. Examination of the function of two kelch proteins generated by stop codon suppression. Development 1997, 124: 1405-1417. PMID: 9118811, DOI: 10.1242/dev.124.7.1405.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAnimalsAnimals, Genetically ModifiedCarrier ProteinsCodon, TerminatorDrosophilaDrosophila ProteinsFemaleGene Expression Regulation, DevelopmentalImmunohistochemistryInfertility, FemaleInsect ProteinsMaleMicrofilament ProteinsMutationOogenesisOpen Reading FramesOvaryRNA, MessengerSuppression, GeneticTissue DistributionConceptsRing canalsKelch proteinStop codon suppressionStop codonCodon suppressionDrosophila kelch geneOvarian ring canalsUGA stop codonFull-length proteinOpen reading frameTissue-specific mannerUAA stop codonFemale sterilitySense codonsReading frameSingle transcriptKelch geneORF1 proteinCodonKelchDifferent tissuesProteinMutantsORF1Transcripts
1994
Cytoskeletal Functions During Drosophila Oogenesis
Cooley L, Theurkauf W. Cytoskeletal Functions During Drosophila Oogenesis. Science 1994, 266: 590-596. PMID: 7939713, DOI: 10.1126/science.7939713.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell DifferentiationCytoplasmDrosophilaFemaleMicrotubulesModels, BiologicalOocytesOogenesisRNA, MessengerConceptsDrosophila oogenesisCytoskeletal functionMature Drosophila oocytesOrganismal morphogenesisDrosophila oocytesCytoskeletal organizationCytoskeletal transformationCell shapeCytoskeletal elementsOogenesisCytological studiesSpecific functionsCell morphologyComplex seriesMechanistic implicationsMechanisms of developmentExperimental approachBasic cytoarchitectureCytoskeletonVersatile systemMorphogenesisCytoplasmOocytesFunctionCellsThe villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis
Mahajan-Miklos S, Cooley L. The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis. Cell 1994, 78: 291-301. PMID: 8044841, DOI: 10.1016/0092-8674(94)90298-4.Peer-Reviewed Original ResearchConceptsVillin-like proteinNurse cellsActin filament bundlesQuail geneMutant egg chambersActin bundle assemblyFilament bundlesEgg chambersFemale sterilityAdult fliesCytoplasmic transportFilamentous actinGene resultsBundle assemblyActin filamentsQuail proteinProtein villinAbsorptive epithelial cellsStriking colocalizationProteinOogenesisVillinEpithelial cellsGenesCells