2021
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 cellsDrosophila
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
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 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 actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeats
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 characteristicsActinScreenUnderstandingOvariesDrosophila 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 growthProteinMutantsSCAR 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
Filamins as integrators of cell mechanics and signalling
Stossel T, Condeelis J, Cooley L, Hartwig J, Noegel A, Schleicher M, Shapiro S. Filamins as integrators of cell mechanics and signalling. Nature Reviews Molecular Cell Biology 2001, 2: 138-145. PMID: 11252955, DOI: 10.1038/35052082.Peer-Reviewed Original ResearchConceptsFilamin geneAmino-terminal actin-binding domainActin filamentsDiverse cellular proteinsActin-binding domainDrosophila filaminCellular proteinsX chromosomeCarboxyl terminusHuman filaminChromosome 3Dictyostelium amoebaeChromosome 7FilaminMembrane receptorsCell mechanicsGenesPeripheral cytoplasmActin gelsSubunitsMutationsFilamentsPeriventricular heterotopiaCell structureDrosophila
2000
Physical and genetic interaction of filamin with presenilin in Drosophila
Guo Y, Zhang S, Sokol N, Cooley L, Boulianne G. Physical and genetic interaction of filamin with presenilin in Drosophila. Journal Of Cell Science 2000, 113: 3499-3508. PMID: 10984440, DOI: 10.1242/jcs.113.19.3499.Peer-Reviewed Original ResearchMeSH KeywordsAlternative SplicingAlzheimer DiseaseAmino Acid SequenceAnimalsBlotting, WesternCarrier ProteinsCloning, MolecularContractile ProteinsDrosophila melanogasterEmbryo, NonmammalianFemaleFilaminsGene Expression Regulation, DevelopmentalHumansInsect ProteinsLarvaMaleMembrane ProteinsMicrofilament ProteinsMolecular Sequence DataPresenilin-1Presenilin-2Protein BindingProtein IsoformsProtein Structure, TertiaryRecombinant Fusion ProteinsRNA, MessengerTwo-Hybrid System TechniquesConceptsN-terminal actin-binding domainOverall amino acid identityOverexpression of presenilinFamilial Alzheimer's diseaseTransmembrane domain proteinActin-binding domainAmino acid identityLarge hydrophilic loopDrosophila filaminDomain proteinsGenetic interactionsAlternative splicingHydrophilic loopAcid identityTerminal domainDrosophilaHuman filaminChromosome 3Spliced formsFilaminAdult phenotypeLoop regionPresenilinNovel familyLong form
1999
Drosophila quail, a villin-related protein, bundles actin filaments in apoptotic nurse cells
Matova N, Mahajan-Miklos S, Mooseker M, Cooley L. Drosophila quail, a villin-related protein, bundles actin filaments in apoptotic nurse cells. Development 1999, 126: 5645-5657. PMID: 10572041, DOI: 10.1242/dev.126.24.5645.Peer-Reviewed Original ResearchMeSH KeywordsActin CytoskeletonActinsAmino Acid SequenceAnimalsApoptosisBiological TransportCalciumCarrier ProteinsCloning, MolecularCytoplasmDrosophila melanogasterEscherichia coliHumansInsect ProteinsMicrofilament ProteinsMolecular Sequence DataRecombinant Fusion ProteinsSequence Homology, Amino AcidConceptsEgg chambersNurse cellsFilamentous actinActin filamentsCytoplasm transportNuclear envelopeQuail proteinGermline-specific proteinsMutant egg chambersNurse cell apoptosisActin bundle assemblyNew actin filamentsApoptotic nurse cellsActin-regulating proteinsBundles actin filamentsHuman villinDrosophila germlineSequence homologyBiochemical experimentsActin bundlesElevated cytoplasmic calciumProteinVillinActinAbundant networkDrosophila 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 ResearchMeSH KeywordsAnimalsContractile ProteinsDrosophilaDrosophila ProteinsFemaleFilaminsInsect ProteinsMicrofilament ProteinsOvaryTissue DistributionConceptsRing 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
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 ResearchMeSH KeywordsActinsAnimalsBinding SitesCarrier ProteinsDNA, ComplementaryDrosophilaFemaleFertilityInsect ProteinsMicrofilament ProteinsMutationOogenesisOvumPhenotypeConceptsActin-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
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
Single Amino Acid Mutations in Drosophila Fascin Disrupt Actin Bundling Function in Vivo
Cant K, Cooley L. Single Amino Acid Mutations in Drosophila Fascin Disrupt Actin Bundling Function in Vivo. Genetics 1996, 143: 249-258. PMID: 8722779, PMCID: PMC1207258, DOI: 10.1093/genetics/143.1.249.Peer-Reviewed Original ResearchConceptsEMS mutagenesis screenMutagenesis screenCytoplasm transportActin-bundling functionDiverse cellular processesIntragenic suppressor mutationsBundles actin filamentsCytoplasmic actin bundlesSingle amino acid mutationSerine 289Glutamic acid resultsAmino acid mutationsDominant suppressorsFascin functionFemale sterileSuppressor mutationsCellular processesC-terminusActin bundlesCentral domainActin filamentsSevere defectsMicrovillar projectionsAcid mutationsFilopodial extensions
1994
Intercellular Cytoplasm Transport during Drosophila Oogenesis
Mahajan-Miklos S, Cooley L. Intercellular Cytoplasm Transport during Drosophila Oogenesis. Developmental Biology 1994, 165: 336-351. PMID: 7958404, DOI: 10.1006/dbio.1994.1257.Peer-Reviewed Original ResearchThe villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis
Mahajan-Miklos S, Cooley L. The villin-like protein encoded by the Drosophila quail gene is required for actin bundle assembly during oogenesis. Cell 1994, 78: 291-301. PMID: 8044841, DOI: 10.1016/0092-8674(94)90298-4.Peer-Reviewed Original ResearchConceptsVillin-like proteinNurse cellsActin filament bundlesQuail geneMutant egg chambersActin bundle assemblyFilament bundlesEgg chambersFemale sterilityAdult fliesCytoplasmic transportFilamentous actinGene resultsBundle assemblyActin filamentsQuail proteinProtein villinAbsorptive epithelial cellsStriking colocalizationProteinOogenesisVillinEpithelial cellsGenesCellsDrosophila 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