2014
Methods 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 dataOogenesisGFPTissue
2011
Reversible 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
Jagunal is required for reorganizing the endoplasmic reticulum during Drosophila oogenesis
Lee S, Cooley L. Jagunal is required for reorganizing the endoplasmic reticulum during Drosophila oogenesis. Journal Of Cell Biology 2007, 176: 941-952. PMID: 17389229, PMCID: PMC2064080, DOI: 10.1083/jcb.200701048.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCaenorhabditis elegansCell DifferentiationConserved SequenceCytoplasmic StreamingDrosophila melanogasterDrosophila ProteinsEndoplasmic ReticulumExocytosisGolgi ApparatusMembrane ProteinsMicroscopy, Electron, TransmissionMolecular Sequence DataOocytesOogenesisProtein TransportSequence Homology, Amino AcidSequence Homology, Nucleic AcidTransport VesiclesZebrafishConceptsVesicular trafficMembrane trafficEndoplasmic reticulumER reorganizationER membrane proteinsDrosophila melanogaster oocytesDrosophila oogenesisMembrane proteinsOocyte endoplasmic reticulumLateral membranesER clusteringReticulumImportant mechanismVitellogenesisOocytesOogenesisEndocytosisReorganizationProteinMembraneCellsThe 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
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 metabolismDiacylglycerolApoptosisAcyltransferaseDrosophilaCellsOogenesis
2000
Eggs to die for: cell death during Drosophila oogenesis
Buszczak M, Cooley L. Eggs to die for: cell death during Drosophila oogenesis. Cell Death & Differentiation 2000, 7: 1071-1074. PMID: 11139280, DOI: 10.1038/sj.cdd.4400755.Peer-Reviewed Original ResearchConceptsGermline apoptosisCell deathDrosophila oogenesisFemale-sterile mutationsSterile mutationsFemale germlineC. elegansGermline cellsGenetic controlDefective cellsEssential nutrientsOogenesisSurviving oocytesApoptosisMorphological changesEggsDrosophilaElegansCellsLater stagesGermlineSpeciesProteinVital roleMutations
1998
Drosophila fascin mutants are rescued by overexpression of the villin-like protein, quail
Cant K, Knowles B, Mahajan-Miklos S, Heintzelman M, Cooley L. Drosophila fascin mutants are rescued by overexpression of the villin-like protein, quail. Journal Of Cell Science 1998, 111: 213-221. PMID: 9405306, DOI: 10.1242/jcs.111.2.213.Peer-Reviewed Original ResearchConceptsActin-bundling proteinActin bundle formationVillin-like proteinBundling proteinNurse cellsActin bundle assemblyCytoplasmic actin bundlesDistinct biochemical propertiesBundle formationCytoplasmic actin networksQuail geneDrosophila germlineDrosophila oogenesisFascin functionGermline transformationEgg chambersCytoplasm transportDrosophila bristlesRedundant functionsActin networkActin bundlesWild typeBundle assemblyQuail proteinSpecialized structures
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
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 ResearchConceptsDrosophila oogenesisCytoskeletal functionMature Drosophila oocytesOrganismal morphogenesisDrosophila oocytesCytoskeletal organizationCytoskeletal transformationCell shapeCytoskeletal elementsOogenesisCytological studiesSpecific functionsCell morphologyComplex seriesMechanistic implicationsMechanisms of developmentExperimental approachBasic cytoarchitectureCytoskeletonVersatile systemMorphogenesisCytoplasmOocytesFunctionCells
1992
chickadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis
Cooley L, Verheyen E, Ayers K. chickadee encodes a profilin required for intercellular cytoplasm transport during Drosophila oogenesis. Cell 1992, 69: 173-184. PMID: 1339308, DOI: 10.1016/0092-8674(92)90128-y.Peer-Reviewed Original ResearchConceptsCytoplasmic actin networksNurse cellsDrosophila oogenesisEgg chambersCytoplasm transportActin networkPolyploid nurse cellsNurse cell nucleiFlow of cytoplasmMutant phenotypeCDNA clonesProtein 40Cytoplasmic contentsAcanthamoeba profilinCell nucleiProfilinNuclear positionOogenesisGenesChickadeesOocytesCellsYeastCytoplasmClones