2023
Evolutionarily conserved midbody remodeling precedes ring canal formation during gametogenesis
Price K, Tharakan D, Cooley L. Evolutionarily conserved midbody remodeling precedes ring canal formation during gametogenesis. Developmental Cell 2023, 58: 474-488.e5. PMID: 36898376, PMCID: PMC10059090, DOI: 10.1016/j.devcel.2023.02.008.Peer-Reviewed Original ResearchConceptsCanal formationStable intercellular bridgesGerm cell divisionMidbody ringTime-lapse imagingFemale germlineCell cytokinesisDrosophila malesRing canalsComplete cytokinesisKinase functionCell divisionCytokinesis eventsBroad functionsCytokinesisIntercellular bridgesExtensive remodelingMidbodyDrosophilaBiological systemsDisease statesImportant insightsGametogenesisGermlineProtein
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-actinCytoskeletonLigaseProteasomeVivoCul3MutagenesisThe Transgenic RNAi Project at Harvard Medical School: Resources and Validation
Perkins LA, Holderbaum L, Tao R, Hu Y, Sopko R, McCall K, Yang-Zhou D, Flockhart I, Binari R, Shim HS, Miller A, Housden A, Foos M, Randkelv S, Kelley C, Namgyal P, Villalta C, Liu LP, Jiang X, Huan-Huan Q, Wang X, Fujiyama A, Toyoda A, Ayers K, Blum A, Czech B, Neumuller R, Yan D, Cavallaro A, Hibbard K, Hall D, Cooley L, Hannon GJ, Lehmann R, Parks A, Mohr SE, Ueda R, Kondo S, Ni JQ, Perrimon N. The Transgenic RNAi Project at Harvard Medical School: Resources and Validation. Genetics 2015, 201: 843-852. PMID: 26320097, PMCID: PMC4649654, DOI: 10.1534/genetics.115.180208.Peer-Reviewed Original Research
2014
Antivirulence Properties of an Antifreeze Protein
Heisig M, Abraham NM, Liu L, Neelakanta G, Mattessich S, Sultana H, Shang Z, Ansari JM, Killiam C, Walker W, Cooley L, Flavell RA, Agaisse H, Fikrig E. Antivirulence Properties of an Antifreeze Protein. Cell Reports 2014, 9: 417-424. PMID: 25373896, PMCID: PMC4223805, DOI: 10.1016/j.celrep.2014.09.034.Peer-Reviewed Original ResearchConceptsAntifreeze proteinsDiverse bacteriaProtein bindsWild-type animalsBiofilm formationAntivirulence agentsIAFGPMethicillin-resistant Staphylococcus aureusHost controlProteinAntifreeze glycoproteinsIxodes scapularisAntivirulence propertiesBacteriaSeptic shockTherapeutic strategiesBacterial infectionsInfectious diseasesMicrobesStaphylococcus aureusFliesBindsInfectionCatheter tubingPathogensMethods 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
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
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
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
UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS
Hudson AM, Cooley L. UNDERSTANDING THE FUNCTION OF ACTIN-BINDING PROTEINS THROUGH GENETIC ANALYSIS OF DROSOPHILA OOGENESIS. Annual Review Of Genetics 2002, 36: 455-488. PMID: 12429700, DOI: 10.1146/annurev.genet.36.052802.114101.Peer-Reviewed Original ResearchConceptsActin-binding proteinsActin cytoskeletonGenetic analysisNew actin-binding proteinCell biological approachesGenetic model systemActin binding proteinsRecent genetic analysesDrosophila ovaryDrosophila oogenesisGenetic screenBiological approachesGenetic resultsProteinCytoskeletonOogenesisModel systemUltrastructural characteristicsActinScreenUnderstandingOvariesMutations 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 metabolismDiacylglycerolApoptosisAcyltransferaseDrosophilaCellsOogenesisControl of DNA Replication and Chromosome Ploidy by Geminin and Cyclin A
Mihaylov IS, Kondo T, Jones L, Ryzhikov S, Tanaka J, Zheng J, Higa LA, Minamino N, Cooley L, Zhang H. Control of DNA Replication and Chromosome Ploidy by Geminin and Cyclin A. Molecular And Cellular Biology 2002, 22: 1868-1880. PMID: 11865064, PMCID: PMC135598, DOI: 10.1128/mcb.22.6.1868-1880.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineCell NucleusCheckpoint Kinase 1ChromosomesCyclin ACyclin BDNADNA ReplicationDNA-Binding ProteinsDown-RegulationDrosophilaDrosophila ProteinsFlow CytometryGene SilencingMolecular Sequence DataPloidiesProtein Kinase InhibitorsProtein KinasesRNA, Double-StrandedSequence Homology, Amino AcidConceptsDNA replicationGeminin deficiencyGenome stabilityCyclin ASingle giant nucleusGiant nucleiCell cycle arrestDrosophila homologueDrosophila cellsGenome instabilityCheckpoint controlChromosome ploidyReplication factorsOverreplicationCyclin BGemininDouble knockoutCycle arrestRapid downregulationDNA contentGenomeSilencingEffect of cyclinHomologuesCyclinDrosophila 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 cytoplasmSubunitsMutationsComplexesSCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila
Zallen JA, Cohen Y, Hudson AM, Cooley L, Wieschaus E, Schejter ED. SCAR is a primary regulator of Arp2/3-dependent morphological events in Drosophila. Journal Of Cell Biology 2002, 156: 689-701. PMID: 11854309, PMCID: PMC2174092, DOI: 10.1083/jcb.200109057.Peer-Reviewed Original ResearchMeSH KeywordsActin-Related Protein 2Actin-Related Protein 3ActinsAmino Acid SequenceAnimalsAxonsBase SequenceBlastodermBrainCytoplasmCytoskeletal ProteinsDNA, ComplementaryDrosophilaDrosophila ProteinsGenes, InsectHumansInsect ProteinsMicrofilament ProteinsMolecular Sequence DataMorphogenesisMutagenesisOogenesisOvumProteinsSequence Homology, Amino AcidWiskott-Aldrich Syndrome ProteinConceptsWiskott-Aldrich syndrome proteinArp2/3 complexAdult eye morphologyScar/WAVECell fate decisionsActin-rich structuresCell biological eventsCortical filamentous actinCell morphologyDrosophila developmentMultiple cell typesNormal cell morphologySCAR homologueFate decisionsSyndrome proteinActin structuresFilamentous actinActin polymerizationCell shapeMorphological eventsCytoplasmic organizationEye morphologyBiological eventsCell typesDevelopmental requirements
2001
Comparative Aspects of Animal Oogenesis
Matova N, Cooley L. Comparative Aspects of Animal Oogenesis. Developmental Biology 2001, 231: 291-320. PMID: 11237461, DOI: 10.1006/dbio.2000.0120.Peer-Reviewed Original Research