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
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 growthProteinMutants
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 formThe kelch repeat superfamily of proteins: propellers of cell function
Adams J, Kelso R, Cooley L, Adams J, Kelso R, Cooley L. The kelch repeat superfamily of proteins: propellers of cell function. Trends In Cell Biology 2000, 10: 17-24. PMID: 10603472, DOI: 10.1016/s0962-8924(99)01673-6.Peer-Reviewed Original ResearchConceptsKelch motifsKelch repeat proteinProtein-protein contact sitesRepeat proteinsTandem elementsMolecular basisORF1 proteinBiological roleContact sitesPolypeptide contextsTertiary structureStructural organizationProteinCell functionMotifDiverse activitiesKelchCurrent informationSequenceCellsMembers
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 network
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
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 interactionsDrosophilaDomainCytoskeletonOogenesisLocalizationSterilityActinExamination 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 tissuesProteinMutantsORF1TranscriptsFormation 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
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
The 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
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