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 ResearchConceptsGermline ring canalsRing canalsActin cytoskeletonF-actinDrosophila melanogaster oogenesisSomatic follicle cellsCombination of CRISPRF-actin accumulationF-actin recruitmentFilamentous actin cytoskeletonFemale germlineActin structuresFruit flyHigh fecundityFollicle cellsCytoskeletonGermlineOverexpressionAccumulationDrosophilaOogenesisMutagenesisCRISPRFilaminGenes
2019
Proximity labeling reveals novel interactomes in live Drosophila tissue
Mannix KM, Starble RM, Kaufman RS, Cooley L. Proximity labeling reveals novel interactomes in live Drosophila tissue. Development 2019, 146: dev176644. PMID: 31208963, PMCID: PMC6679357, DOI: 10.1242/dev.176644.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAnimalsAnimals, Genetically ModifiedCell CommunicationCell DifferentiationCytological TechniquesCytoskeletonDNA-(Apurinic or Apyrimidinic Site) LyaseDrosophila melanogasterFemaleGenes, ReporterGerm CellsIntercellular JunctionsMolecular ImagingOocytesOogenesisProtein BindingProtein Interaction MapsStaining and LabelingConceptsProximity labelingIntercellular bridgesProximity-dependent biotinylationStable intercellular bridgesRC proteinDynamic actin cytoskeletonProtein interactome analysisRNA interference screenNovel interactomePrey genesUncharacterized proteinsDistinct interactomesDrosophila tissuesActin cytoskeletonInterference screenInteractome analysisLive tissueMultiple proteinsProximity ligationInteractomeGerm cellsIntercellular communicationRespective preyFunctional roleProtein
2015
Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase
Hudson AM, Mannix KM, Cooley L. Actin Cytoskeletal Organization in Drosophila Germline Ring Canals Depends on Kelch Function in a Cullin-RING E3 Ligase. Genetics 2015, 201: 1117-1131. PMID: 26384358, PMCID: PMC4649639, DOI: 10.1534/genetics.115.181289.Peer-Reviewed Original ResearchConceptsKelch functionE3 ligaseCullin-RING E3 ligaseGermline ring canalsActin cytoskeletal organizationDrosophila kelch proteinUbiquitin ligase activityCross-link F-actinUbiquitin E3 ligaseRing canalsKelch proteinProtein substratesCytoskeletal defectsCytoskeletal organizationCytoskeletal remodelingLigase activityCullin 3KelchF-actinCytoskeletonLigaseProteasomeVivoCul3Mutagenesis
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 responseA Regulatory Network of Drosophila Germline Stem Cell Self-Renewal
Yan D, Neumüller RA, Buckner M, Ayers K, Li H, Hu Y, Yang-Zhou D, Pan L, Wang X, Kelley C, Vinayagam A, Binari R, Randklev S, Perkins LA, Xie T, Cooley L, Perrimon N. A Regulatory Network of Drosophila Germline Stem Cell Self-Renewal. Developmental Cell 2014, 28: 459-473. PMID: 24576427, PMCID: PMC3998650, DOI: 10.1016/j.devcel.2014.01.020.Peer-Reviewed Original ResearchConceptsGermline stem cellsSelf-renewal factorsDrosophila female germline stem cellsStem cellsDifferent stem cell lineagesLarge-scale RNAi screenFemale germline stem cellsLoss of Set1Stem Cell Self-RenewalSpecific genetic networksHistone methyltransferase Set1Stem cell identityCell fate decisionsStem cell lineagesCell Self-RenewalSelf-renewal genesRNAi screenDistinct fatesFate decisionsGSC maintenanceCell identityCell fateRegulatory networksGenetic networksNeural stem cellsMethods for studying oogenesis
Hudson AM, Cooley L. Methods for studying oogenesis. Methods 2014, 68: 207-217. PMID: 24440745, PMCID: PMC4048766, DOI: 10.1016/j.ymeth.2014.01.005.Peer-Reviewed Original ResearchConceptsGAL4/UAS systemStem cell maintenanceDevelopmental cell biologyCell cycle controlClonal screensDrosophila oogenesisCell polarityWhole-mount tissuesCytoskeletal regulationEgg chambersTransgenic linesCell maintenanceIntercellular transportSomatic cellsTrap linesGamete developmentCell biologyUAS systemExcellent systemCycle controlGene expressionIntercellular communicationCell deathOogenesisCell migration
2013
Bridging the divide
McLean PF, Cooley L. Bridging the divide. Fly 2013, 8: 13-18. PMID: 24406334, PMCID: PMC3974888, DOI: 10.4161/fly.27016.Peer-Reviewed Original ResearchConceptsRing canalsMitotic clonesSomatic tissuesDrosophila somatic tissuesFollicle cellsProtein of interestNon-recombined cellsDirect cytoplasmic connectionsDrosophila oogenesisImaginal discsGenetic toolsIntercellular exchangeProtein movementCleavage furrowCytoplasmic connectionsProteinClonesCellsMosaic cellsClonal dataOogenesisGFPTissueProtein Equilibration Through Somatic Ring Canals in Drosophila
McLean PF, Cooley L. Protein Equilibration Through Somatic Ring Canals in Drosophila. Science 2013, 340: 1445-1447. PMID: 23704373, PMCID: PMC3819220, DOI: 10.1126/science.1234887.Peer-Reviewed Original ResearchConceptsRing canalsLarval imaginal discsDrosophila ovaryClone boundariesImaginal discsIncomplete cytokinesisIntercellular communicationCytoplasmic contentsFollicle cellsIntercellular bridgesTissue biologyProtein expressionConnected cellsDrosophilaCytokinesisCellsBiologyProteinTissueExpressionOvaries
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
2011
Intercellular protein movement in syncytial Drosophila follicle cells
Airoldi SJ, McLean PF, Shimada Y, Cooley L. Intercellular protein movement in syncytial Drosophila follicle cells. Journal Of Cell Science 2011, 124: 4077-4086. PMID: 22135360, PMCID: PMC3244987, DOI: 10.1242/jcs.090456.Peer-Reviewed Original ResearchConceptsImaginal disc cellsRing canalsFollicle cellsPavarotti kinesin-like proteinDrosophila follicle cellsIntercellular protein movementEgg chamber developmentKinesin-like proteinMitotic cleavage furrowsLive-cell confocal microscopyDisc cellsBroad functional significanceDrosophila germlineGermline cellsCytoplasmic proteinsSomatic cellsProtein movementCleavage furrowFunctional significanceChamber developmentSyncytial organizationConfocal microscopyGermlineProteinCellsReversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis
Shimada Y, Burn KM, Niwa R, Cooley L. Reversible response of protein localization and microtubule organization to nutrient stress during Drosophila early oogenesis. Developmental Biology 2011, 355: 250-262. PMID: 21570389, PMCID: PMC3118931, DOI: 10.1016/j.ydbio.2011.04.022.Peer-Reviewed Original ResearchConceptsEgg chambersNutrient stressIntercellular transportMT reorganizationNutrient availabilityNurse cellsPutative RNA binding proteinMT-dependent mannerRNA binding proteinYpsilon SchachtelDrosophila oogenesisProcessing bodiesProtein localizationEarly oogenesisNutrient deprivationMicrotubule organizationMetabolic checkpointCytoplasmic componentsAnimal oocytesStress responseYolk uptakeBinding proteinPrevitellogenic stageOogenesisIndependent mechanisms
2010
Drosophila 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 ResearchConceptsDrosophila 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 actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeats
2007
Mononuclear muscle cells in Drosophila ovaries revealed by GFP protein traps
Hudson AM, Petrella LN, Tanaka AJ, Cooley L. Mononuclear muscle cells in Drosophila ovaries revealed by GFP protein traps. Developmental Biology 2007, 314: 329-340. PMID: 18199432, PMCID: PMC2293129, DOI: 10.1016/j.ydbio.2007.11.029.Peer-Reviewed Original ResearchConceptsMuscle specificationEpithelial sheath cellsMyoblast fusionSheath cellsProtein trapSarcomere organizationFLP/FRT systemMononuclear muscle cellsMuscle cellsDrosophila ovaryGonadal mesodermGenetic mosaicsKey genesTrap linesFRT systemGenetic analysisHuman muscle physiologySomatic musclesVisceral musclesSingle nucleusClonal analysisFemale reproductive systemMuscle physiologyEpithelial sheathModel systemThe Ovhts polyprotein is cleaved to produce fusome and ring canal proteins required for Drosophila oogenesis
Petrella LN, Smith-Leiker T, Cooley L. The Ovhts polyprotein is cleaved to produce fusome and ring canal proteins required for Drosophila oogenesis. Development 2007, 134: 703-712. PMID: 17215303, DOI: 10.1242/dev.02766.Peer-Reviewed Original ResearchConceptsDrosophila oogenesisRing canalsFemale sterile mutantPost-mitotic cellsDrosophila adducinSpecialized organellesEarly oogenesisLate oogenesisHT proteinsFusomeMitotic proliferationHT genesMitotic cellsOogenesisGerm cellsNormal developmentCell proliferationProteinPolyproteinCellsEssential componentProliferationMutantsAdducinOrganelles
2006
Illuminating the role of caspases during Drosophila oogenesis
Mazzalupo S, Cooley L. Illuminating the role of caspases during Drosophila oogenesis. Cell Death & Differentiation 2006, 13: 1950-1959. PMID: 16528381, DOI: 10.1038/sj.cdd.4401892.Peer-Reviewed Original ResearchConceptsNurse cell deathCaspase activityCell deathNurse cellsFluorescent proteinApoptosis protein 1Caspase inhibitor p35Caspase cleavage siteStarvation-induced deathRole of caspasesStarvation-induced apoptosisCyan fluorescent proteinYellow fluorescent proteinDrosophila inhibitorGermline developmentDrosophila oogenesisNormal oogenesisPoor environmental conditionsOogenesisCleavage siteProtein 1Environmental conditionsCaspasesProteinOocytes
2005
Drosophila myosin V is required for larval development and spermatid individualization
Mermall V, Bonafé N, Jones L, Sellers JR, Cooley L, Mooseker MS. Drosophila myosin V is required for larval development and spermatid individualization. Developmental Biology 2005, 286: 238-255. PMID: 16126191, DOI: 10.1016/j.ydbio.2005.07.028.Peer-Reviewed Original ResearchConceptsInvestment conesLarval developmentClass V myosinsIndividualization complexSpermatid individualizationCytological defectsTruncation alleleVesicular trafficRNA transportActin structuresLarval tissuesMutant animalsMature spermSperm nucleiMyoVSpermatid maturationMolecular motorsMyosin VMechanochemical couplingDetectable defectsV geneMicrotubulesIndividual membranesActinSpermatogenesis
2003
Drosophila filamin is required for follicle cell motility during oogenesis
Sokol NS, Cooley L. Drosophila filamin is required for follicle cell motility during oogenesis. Developmental Biology 2003, 260: 260-272. PMID: 12885568, DOI: 10.1016/s0012-1606(03)00248-3.Peer-Reviewed Original ResearchConceptsGermline cystsFilamin proteinsCell motilityFollicle cell morphogenesisActin-binding domainActin binding proteinsFilamin repeatsDrosophila ovaryFilamin functionCell morphogenesisDrosophila filaminFilamin familyCell movementProtein 120Cell shapeBorder cellsCell locomotionFollicle cellsBinding proteinPoint mutationsInitial encapsulationProteinMorphogenesisReduced expressionFilamin
2002
Mutations in the midway Gene Disrupt a Drosophila Acyl Coenzyme A: Diacylglycerol Acyltransferase
Buszczak M, Lu X, Segraves WA, Chang TY, Cooley L. Mutations in the midway Gene Disrupt a Drosophila Acyl Coenzyme A: Diacylglycerol Acyltransferase. Genetics 2002, 160: 1511-1518. PMID: 11973306, PMCID: PMC1462074, DOI: 10.1093/genetics/160.4.1511.Peer-Reviewed Original ResearchConceptsEgg chambersDiacylglycerol acyltransferaseNurse cellsAcyl coenzyme AMutant egg chambersNurse cell deathCell deathInsect cells resultsEgg chamber developmentCoenzyme AGermline apoptosisDrosophila oogenesisCytoplasm transportDGAT activityCells resultsChamber developmentNeutral lipidsGenesLipid metabolismDiacylglycerolApoptosisAcyltransferaseDrosophilaCellsOogenesisDrosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation
Kelso RJ, Hudson AM, Cooley L. Drosophila Kelch regulates actin organization via Src64-dependent tyrosine phosphorylation. Journal Of Cell Biology 2002, 156: 703-713. PMID: 11854310, PMCID: PMC2174084, DOI: 10.1083/jcb.200110063.Peer-Reviewed Original ResearchMeSH KeywordsActinsAlanineAmino Acid SequenceAnimalsCarrier ProteinsCross-Linking ReagentsDrosophilaDrosophila ProteinsFemaleInsect ProteinsMicrofilament ProteinsMicroscopy, ElectronMolecular Sequence DataMutagenesis, Site-DirectedPhosphorylationProtein-Tyrosine KinasesProto-Oncogene ProteinsRecombinant Fusion ProteinsSequence Homology, Amino AcidSignal TransductionTyrosineConceptsRing canalsActin organizationDrosophila kelch geneOvarian ring canalsRing canal growthActin cross-linking activitySite-directed mutagenesisTwo-dimensional electrophoresisActin binding siteKelch functionDrosophila KelchCross-linking activityProper morphogenesisKelch proteinTyrosine phosphorylationKelch geneNegative regulationRepeat 5KelchActin filamentsResidue 627Biochemical studiesCanal growthProteinMutantsA subset of dynamic actin rearrangements in Drosophila requires the Arp2/3 complex
Hudson AM, Cooley L. A subset of dynamic actin rearrangements in Drosophila requires the Arp2/3 complex. Journal Of Cell Biology 2002, 156: 677-687. PMID: 11854308, PMCID: PMC2174088, DOI: 10.1083/jcb.200109065.Peer-Reviewed Original ResearchConceptsArp2/3 complexRing canal growthActin-related proteinsParallel actin bundlesNurse cell cytoplasmActin filament nucleationDynamic actin rearrangementsActin cytoskeletonRing canalsActin structuresSlow spontaneous rateActin rearrangementPupal epitheliumPlasma membraneFilament nucleationShaft cellsActin bundlesActin filamentsComplex contributesFunction mutationsCanal growthCell cytoplasmSubunitsMutationsComplexes