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
2012
Expression of Ixodes scapularis Antifreeze Glycoprotein Enhances Cold Tolerance in Drosophila melanogaster
Neelakanta G, Hudson AM, Sultana H, Cooley L, Fikrig E. Expression of Ixodes scapularis Antifreeze Glycoprotein Enhances Cold Tolerance in Drosophila melanogaster. PLOS ONE 2012, 7: e33447. PMID: 22428051, PMCID: PMC3302814, DOI: 10.1371/journal.pone.0033447.Peer-Reviewed Original ResearchMeSH KeywordsAcclimatizationAnalysis of VarianceAnimalsAnimals, Genetically ModifiedAntifreeze ProteinsApoptosisCold TemperatureDrosophila melanogasterEmbryo, NonmammalianEnzyme-Linked Immunosorbent AssayFemaleImmunoblottingIn Situ Nick-End LabelingIxodesMaleMusclesOligonucleotidesReal-Time Polymerase Chain ReactionConceptsNon-freezing temperaturesD. melanogasterDrosophila melanogasterCold toleranceLow non-freezing temperaturesFemale adult fliesTransgenic D. melanogasterCold shock injuryAbility of fliesAntifreeze glycoproteinsAdult fliesMolecular basisMelanogasterFlight musclesFliesAntifreeze proteinsHatching rateHigher survival rateApoptotic damageGlycoproteinExpressionToleranceEmbryosProteinApoptosis
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 disordersMutationsPhenotypeArp2/3-Dependent Psuedocleavage Furrow Assembly in Syncytial Drosophila Embryos
Stevenson V, Hudson A, Cooley L, Theurkauf WE. Arp2/3-Dependent Psuedocleavage Furrow Assembly in Syncytial Drosophila Embryos. Current Biology 2002, 12: 705-711. PMID: 12007413, DOI: 10.1016/s0960-9822(02)00807-2.Peer-Reviewed Original ResearchConceptsDrosophila embryosPseudocleavage furrowsCell cycleActin capActin reorganizationSomatic cell divisionLocal actin polymerizationSyncytial Drosophila embryosARPC1 subunitArp2/3 complexNuclear positioningEmbryonic divisionsComplex localizeCell divisionActin polymerizationCleavage furrowFurrow formationCap functionSpindle fusionMolecular mechanismsArp2/3EmbryosVivo analysisMutationsAssembly
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