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
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 metabolismDiacylglycerolApoptosisAcyltransferaseDrosophilaCellsOogenesisSCAR 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
2000
Eggs to die for: cell death during Drosophila oogenesis
Buszczak M, Cooley L. Eggs to die for: cell death during Drosophila oogenesis. Cell Death & Differentiation 2000, 7: 1071-1074. PMID: 11139280, DOI: 10.1038/sj.cdd.4400755.Peer-Reviewed Original ResearchConceptsGermline apoptosisCell deathDrosophila oogenesisFemale-sterile mutationsSterile mutationsFemale germlineC. elegansGermline cellsGenetic controlDefective cellsEssential nutrientsOogenesisSurviving oocytesApoptosisMorphological changesEggsDrosophilaElegansCellsLater stagesGermlineSpeciesProteinVital roleMutationsPhysical 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
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 bindingThe extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation.
Schaack J, Sharp S, Dingermann T, Burke DJ, Cooley L, Söll D. The extent of a eukaryotic tRNA gene. 5‘- and 3‘-flanking sequence dependence for transcription and stable complex formation. Journal Of Biological Chemistry 1984, 259: 1461-1467. PMID: 6693417, DOI: 10.1016/s0021-9258(17)43429-6.Peer-Reviewed Original ResearchConceptsStable complex formationBase pairsDrosophila Kc cell extractSequence requirementsCell extractsEukaryotic tRNA genesStable transcription complexesHeLa cell extractsTRNA genesComplex formationTranscription complexArg genesEfficient transcriptionTranscription assaysTranscription propertiesCell-free extractsTranscriptionHomologous systemGenesSequenceSequence dependenceCellular sourceExtractAssaysPairs