Featured Publications
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 cellsDrosophilaTargeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion
Hudson AM, Mannix KM, Gerdes JA, Kottemann MC, Cooley L. Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion. Development 2018, 146: dev169219. PMID: 30559276, PMCID: PMC6340150, DOI: 10.1242/dev.169219.Peer-Reviewed Original ResearchConceptsTandem affinity purificationUbiquitin ligase complexCullin-3 functionShort sequence motifsSpecialized cytoskeletal structuresUbiquitin-proteasome systemF-actin cytoskeletonSpecialized actinLigase complexActin cytoskeletonRing canalsSequence motifsGenetic evidenceCytoskeletal structuresAffinity purificationCytoskeletonSubstrate degradationBiochemical evidenceUnusual mechanismKelchCRL3CullinMass spectrometryOogenesisMutagenesisDrosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton
Hudson AM, Cooley L. Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton. Journal Of Cell Biology 2010, 188: 29-37. PMID: 20065088, PMCID: PMC2812842, DOI: 10.1083/jcb.200909017.Peer-Reviewed Original ResearchMeSH KeywordsActinsAnimalsCell DifferentiationCullin ProteinsCytoskeletonDrosophila melanogasterDrosophila ProteinsFemaleMicrofilament ProteinsOvumProtein BindingConceptsDrosophila KelchCullin 3Cullin-RING ubiquitin E3 ligasesGermline ring canalsSubstrate adaptor proteinCullin-RING ligaseDiverse protein familiesF-actin cytoskeletal structureUbiquitin E3 ligasesProtein ubiquitylationActin cytoskeletonE3 ligasesRing canalsAdaptor proteinProtein familySequence motifsCytoskeletal structuresFilamentous actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeatsArp2/3-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 analysisMutationsAssemblyP element homing to the Drosophila bithorax complex
Bender W, Hudson A. P element homing to the Drosophila bithorax complex. Development 2000, 127: 3981-3992. PMID: 10952896, DOI: 10.1242/dev.127.18.3981.Peer-Reviewed Original ResearchAnimalsDNA NucleotidyltransferasesDNA Transposable ElementsDNA-Binding ProteinsDrosophila melanogasterDrosophila ProteinsGene Expression RegulationGenes, InsectGenes, ReporterHomeodomain ProteinsImmunohistochemistryMutationPhenotypePhysical Chromosome MappingRecombination, GeneticRNA, MessengerTranscription Factors
2020
HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis
Gerdes JA, Mannix KM, Hudson AM, Cooley L. HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis. Genetics 2020, 216: 717-734. PMID: 32883702, PMCID: PMC7648574, DOI: 10.1534/genetics.120.303629.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAnimalsCalmodulin-Binding ProteinsCytokinesisDrosophila melanogasterDrosophila ProteinsFemaleFilaminsOogenesisOvumConceptsGermline ring canalsRing canalsActin cytoskeletonF-actinDrosophila melanogaster oogenesisSomatic follicle cellsCombination of CRISPRF-actin accumulationF-actin recruitmentFilamentous actin cytoskeletonFemale germlineActin structuresFruit flyHigh fecundityFollicle cellsCytoskeletonGermlineOverexpressionAccumulationDrosophilaOogenesisMutagenesisCRISPRFilaminGenesDrosophila sperm development and intercellular cytoplasm sharing through ring canals do not require an intact fusome
Kaufman RS, Price KL, Mannix KM, Ayers KM, Hudson AM, Cooley L. Drosophila sperm development and intercellular cytoplasm sharing through ring canals do not require an intact fusome. Development 2020, 147: dev190140. PMID: 33033119, PMCID: PMC7687857, DOI: 10.1242/dev.190140.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCytoplasmDrosophila melanogasterMaleMeiosisSpermatidsSpermatogenesisSpermatogoniaConceptsRing canalsSperm developmentPost-meiotic haploid spermatidsGerm cellsGermline ring canalsAnimal germ cellsQuality control surveillanceLarge cytoplasmic structuresCytoplasmic informationDiploid spermatogoniaHaploid spermatidsSpecialized organellesIncomplete cytokinesisIntercellular movementCell divisionEndogenous proteinsFusomeCytoplasmic structuresIntercellular bridgesMale fertilityIntercellular trafficSpermatogenesisCellsCytokinesisNormal conditions
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
2007
Exploring Strategies for Protein Trapping in Drosophila
Quiñones-Coello A, Petrella LN, Ayers K, Melillo A, Mazzalupo S, Hudson AM, Wang S, Castiblanco C, Buszczak M, Hoskins RA, Cooley L. Exploring Strategies for Protein Trapping in Drosophila. Genetics 2007, 175: 1089-1104. PMID: 17179094, PMCID: PMC1840052, DOI: 10.1534/genetics.106.065995.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein trapEnhancer trapFluorescent proteinExpression dataGFP expressionGFP fusion proteinFluorescent protein tagsCell biological studiesProduction of GFPWeb-accessible databaseChromosomal positionProtein tagsProtein trappingEndogenous proteinsGenomic DNASplice acceptorDonor sequenceNew insertionsMolecular informationGenesProteinDrosophilaTransposonBiological studies
1997
Formation of the Drosophila Ovarian Ring Canal Inner Rim Depends on cheerio
Robinson D, Smith-Leiker T, Sokol N, Hudson A, Cooley L. Formation of the Drosophila Ovarian Ring Canal Inner Rim Depends on cheerio. Genetics 1997, 145: 1063-1072. PMID: 9093858, PMCID: PMC1207876, DOI: 10.1093/genetics/145.4.1063.Peer-Reviewed Original ResearchMeSH KeywordsActinsAllelesAnimalsCalmodulin-Binding ProteinsCarrier ProteinsCell CommunicationCell MembraneChromosome MappingCytoskeletonDrosophila melanogasterDrosophila ProteinsFemaleGene Expression Regulation, DevelopmentalGenes, InsectInfertility, FemaleInsect ProteinsIntercellular JunctionsMicrofilament ProteinsOocytesOvaryConceptsStable intercellular bridgesExamination of mutantsDrosophila oogenesisPlasma membrane stabilizationRing canalsCytoplasm transportMutant cellsFilamentous actinCleavage furrowRIM proteinsNurse cellsActin filamentsIntercellular bridgesMutantsCritical functionsKelchCheeriosProteinStep-wise processAssemblyMembrane stabilizationCellsCytoskeletonOogenesisGenes