2008
Phylogenetic, Structural and Functional Relationships between WD- and Kelch-Repeat Proteins
Hudson AM, Cooley L. Phylogenetic, Structural and Functional Relationships between WD- and Kelch-Repeat Proteins. Subcellular Biochemistry 2008, 48: 6-19. PMID: 18925367, DOI: 10.1007/978-0-387-09595-0_2.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceModels, MolecularMolecular Sequence DataPhylogenyProtein ConformationProteinsRepetitive Sequences, Amino AcidSequence Homology, Amino AcidConceptsΒ-propeller proteinsKelch repeat proteinWidespread protein familyWD-repeat proteinΒ-propeller structureΒ-propeller foldΒ-propeller domainWD repeatsMolecular functionsCommon ancestorProtein familyEvolutionary advantageDiverse familySimilar functionsProteinΒ-sheetKelchStructural motifsRepeat unitsExhibit similaritiesMotifFunctional relationshipFamilySuperfamilyAncestor
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 mechanismVitellogenesisOocytesOogenesisEndocytosisReorganizationProteinMembraneCells
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
Mutations 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 metabolismDiacylglycerolApoptosisAcyltransferaseDrosophilaCellsOogenesisControl of DNA Replication and Chromosome Ploidy by Geminin and Cyclin A
Mihaylov IS, Kondo T, Jones L, Ryzhikov S, Tanaka J, Zheng J, Higa LA, Minamino N, Cooley L, Zhang H. Control of DNA Replication and Chromosome Ploidy by Geminin and Cyclin A. Molecular And Cellular Biology 2002, 22: 1868-1880. PMID: 11865064, PMCID: PMC135598, DOI: 10.1128/mcb.22.6.1868-1880.2002.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCell Cycle ProteinsCell LineCell NucleusCheckpoint Kinase 1ChromosomesCyclin ACyclin BDNADNA ReplicationDNA-Binding ProteinsDown-RegulationDrosophilaDrosophila ProteinsFlow CytometryGene SilencingMolecular Sequence DataPloidiesProtein Kinase InhibitorsProtein KinasesRNA, Double-StrandedSequence Homology, Amino AcidConceptsDNA replicationGeminin deficiencyGenome stabilityCyclin ASingle giant nucleusGiant nucleiCell cycle arrestDrosophila homologueDrosophila cellsGenome instabilityCheckpoint controlChromosome ploidyReplication factorsOverreplicationCyclin BGemininDouble knockoutCycle arrestRapid downregulationDNA contentGenomeSilencingEffect of cyclinHomologuesCyclinA 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 cytoplasmSubunitsMutationsComplexesSCAR 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 requirementsDrosophila 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
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 cellsGenesCells
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
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
1984
Transcription factor binding is limited by the 5'-flanking regions of a Drosophila tRNAHis gene and a tRNAHis pseudogene.
Cooley L, Schaack J, Burke DJ, Thomas B, Söll D. Transcription factor binding is limited by the 5'-flanking regions of a Drosophila tRNAHis gene and a tRNAHis pseudogene. Molecular And Cellular Biology 1984, 4: 2714-2722. PMID: 6570190, PMCID: PMC369281, DOI: 10.1128/mcb.4.12.2714.Peer-Reviewed Original ResearchConceptsDrosophila Kc cell extractHeLa cell extractsCell extractsReal genesStable complex formationControl regionDeletion analysisStable transcription complex formationRecombinant clonesDrosophila tRNAArg geneTRNA gene clusterTranscription complex formationBona fide genesInternal control regionTranscription factor bindingSame DNA strandComplex formationTranscription control regionsConsecutive base pairsTRNAHis geneTRNAArg geneFide genesGene clusterTranscription factorsFactor binding