2007
Exploring Strategies for Protein Trapping in Drosophila
Quiñones-Coello A, Petrella LN, Ayers K, Melillo A, Mazzalupo S, Hudson AM, Wang S, Castiblanco C, Buszczak M, Hoskins RA, Cooley L. Exploring Strategies for Protein Trapping in Drosophila. Genetics 2007, 175: 1089-1104. PMID: 17179094, PMCID: PMC1840052, DOI: 10.1534/genetics.106.065995.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein trapEnhancer trapFluorescent proteinExpression dataGFP expressionGFP fusion proteinFluorescent protein tagsCell biological studiesProduction of GFPWeb-accessible databaseChromosomal positionProtein tagsProtein trappingEndogenous proteinsGenomic DNASplice acceptorDonor sequenceNew insertionsMolecular informationGenesProteinDrosophilaTransposonBiological studies
2004
Flytrap, a database documenting a GFP protein‐trap insertion screen in Drosophila melanogaster
Kelso RJ, Buszczak M, Quiñones AT, Castiblanco C, Mazzalupo S, Cooley L. Flytrap, a database documenting a GFP protein‐trap insertion screen in Drosophila melanogaster. Nucleic Acids Research 2004, 32: d418-d420. PMID: 14681446, PMCID: PMC308749, DOI: 10.1093/nar/gkh014.Peer-Reviewed Original ResearchConceptsProtein localizationInsertion linesDrosophila melanogasterGFP fusion proteinTransposable element insertionsCellular component ontologyGene Ontology ConsortiumTransposable P elementsInverse PCR productsGene intronsArtificial exonElement insertionsGenomic DNAFusion proteinFlytrapMelanogasterComponent ontologyP elementsStages of developmentType of tissueLocalizationFlyBaseIntronsExonsGenes
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 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 network