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
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 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 ResearchConceptsRing 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
2018
Targeted 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 spectrometryOogenesisMutagenesis
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
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 microscopyGermlineProteinCells
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
The 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
2002
Drosophila 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
1999
Drosophila Filamin encoded by the cheerio locus is a component of ovarian ring canals
Sokol N, Cooley L. Drosophila Filamin encoded by the cheerio locus is a component of ovarian ring canals. Current Biology 1999, 9: 1221-1230. PMID: 10556087, DOI: 10.1016/s0960-9822(99)80502-8.Peer-Reviewed Original ResearchConceptsRing canalsDrosophila filaminPlasma membraneFilamentous actinActin filamentsOvarian ring canalsFruit fly DrosophilaLoss of filaminActin-binding domainActin-binding proteinsParallel actin bundlesLocalization of filaminFlow of cytoplasmFly DrosophilaActin structuresFilamin isoformsTransmembrane proteinCell cortexActin arraysContractile ringKelch geneCytoskeletal proteinsCleavage furrowStress fibersActin bundles
1997
Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer
Robinson D, Cooley L. Drosophila Kelch Is an Oligomeric Ring Canal Actin Organizer. Journal Of Cell Biology 1997, 138: 799-810. PMID: 9265647, PMCID: PMC2138045, DOI: 10.1083/jcb.138.4.799.Peer-Reviewed Original ResearchConceptsDrosophila KelchRing canalsAmino halfKelch repeat domainStructure-function analysisAmino-terminal regionGerm cell membranesKelch family proteinDominant sterilityBTB domainProtein domainsRepeat domainKelchActin filamentsCell membraneProteinCanal localizationAdditional interactionsDrosophilaDomainCytoskeletonOogenesisLocalizationSterilityActinFormation 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 stabilizationCellsCytoskeletonOogenesisGenesExamination of the function of two kelch proteins generated by stop codon suppression
Robinson D, Cooley L. Examination of the function of two kelch proteins generated by stop codon suppression. Development 1997, 124: 1405-1417. PMID: 9118811, DOI: 10.1242/dev.124.7.1405.Peer-Reviewed Original ResearchMeSH KeywordsAlanineAnimalsAnimals, Genetically ModifiedCarrier ProteinsCodon, TerminatorDrosophilaDrosophila ProteinsFemaleGene Expression Regulation, DevelopmentalImmunohistochemistryInfertility, FemaleInsect ProteinsMaleMicrofilament ProteinsMutationOogenesisOpen Reading FramesOvaryRNA, MessengerSuppression, GeneticTissue DistributionConceptsRing canalsKelch proteinStop codon suppressionStop codonCodon suppressionDrosophila kelch geneOvarian ring canalsUGA stop codonFull-length proteinOpen reading frameTissue-specific mannerUAA stop codonFemale sterilitySense codonsReading frameSingle transcriptKelch geneORF1 proteinCodonKelchDifferent tissuesProteinMutantsORF1Transcripts
1996
Stable intercellular bridges in development: the cytoskeleton lining the tunnel
Robinson D, Cooley L. Stable intercellular bridges in development: the cytoskeleton lining the tunnel. Trends In Cell Biology 1996, 6: 474-479. PMID: 15157506, DOI: 10.1016/0962-8924(96)84945-2.Peer-Reviewed Original ResearchStable intercellular bridgesIntercellular bridgesIntercellular junctionsExamination of mutantsDrosophila germlineRing canalsSignal transductionIntercellular transportCytoplasmic connectionsCell adhesionAssemblyCytoskeletonMutantsOrganellesGermlineTransductionOrganismsCytoplasmWide varietyCellsRapid transferAdhesionJunction
1994
Morphogenesis of Drosophila ovarian ring canals
Robinson D, Cant K, Cooley L. Morphogenesis of Drosophila ovarian ring canals. Development 1994, 120: 2015-2025. PMID: 7925006, DOI: 10.1242/dev.120.7.2015.Peer-Reviewed Original ResearchConceptsRing canalsEgg chambersHu-li tai shaoMutant egg chambersOvarian ring canalsEgg chamber developmentDrosophila egg chamberCanal developmentCarboxy-terminal tailCytoskeletal protein assemblyAnti-phosphotyrosine antibodyProtein assembliesHT proteinsTyrosine phosphorylationFilamentous actinCytoplasmic bridgesActinChamber developmentKelchProteinCanal componentsAssemblyMorphogenesisGermariumPhosphorylationDrosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension.
Cant K, Knowles BA, Mooseker MS, Cooley L. Drosophila singed, a fascin homolog, is required for actin bundle formation during oogenesis and bristle extension. Journal Of Cell Biology 1994, 125: 369-380. PMID: 8163553, PMCID: PMC2120035, DOI: 10.1083/jcb.125.2.369.Peer-Reviewed Original ResearchConceptsActin filament bundle formationActin filament bundlesSevere mutantsBundle formationFilament bundlesActin bundle formationBundles actin filamentsNurse cell nucleiDrosophila homologBristle phenotypeSocket cellsFemale sterileEgg chambersRing canalsCytoplasm transportSea urchin eggsNurse cellsActin bundlesCellular extensionsSevere allelesActin filamentsDrosophilaMutantsMigratory cellsFilopodial extensions
1993
Kelch encodes a component of intercellular bridges in Drosophila egg chambers
Xue F, Cooley L. Kelch encodes a component of intercellular bridges in Drosophila egg chambers. Cell 1993, 72: 681-693. PMID: 8453663, DOI: 10.1016/0092-8674(93)90397-9.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBiological TransportCarrier ProteinsConserved SequenceDrosophilaDrosophila ProteinsGerm CellsIntercellular JunctionsMicrofilament ProteinsMolecular Sequence DataOogenesisOpen Reading FramesRepetitive Sequences, Nucleic AcidSequence Homology, Amino AcidConceptsRing canalsIntercellular bridgesFemale-sterile mutationsDrosophila egg chamberUGA stop codonOpen reading frameFlow of cytoplasmSterile mutationsEgg chambersLong proteinShorter proteinCytoplasm transportORF1 productUGA codonReading frameKelch geneUnusual transcriptsNurse cellsProtein productsStop codonKelchOocyte maturationCodonORF1Cytoplasm