Featured Publications
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-actinCytoskeletonLigaseProteasomeVivoCul3MutagenesisMethods for studying oogenesis
Hudson AM, Cooley L. Methods for studying oogenesis. Methods 2014, 68: 207-217. PMID: 24440745, PMCID: PMC4048766, DOI: 10.1016/j.ymeth.2014.01.005.Peer-Reviewed Original ResearchConceptsGAL4/UAS systemStem cell maintenanceDevelopmental cell biologyCell cycle controlClonal screensDrosophila oogenesisCell polarityWhole-mount tissuesCytoskeletal regulationEgg chambersTransgenic linesCell maintenanceIntercellular transportSomatic cellsTrap linesGamete developmentCell biologyUAS systemExcellent systemCycle controlGene expressionIntercellular communicationCell deathOogenesisCell migrationMononuclear muscle cells in Drosophila ovaries revealed by GFP protein traps
Hudson AM, Petrella LN, Tanaka AJ, Cooley L. Mononuclear muscle cells in Drosophila ovaries revealed by GFP protein traps. Developmental Biology 2007, 314: 329-340. PMID: 18199432, PMCID: PMC2293129, DOI: 10.1016/j.ydbio.2007.11.029.Peer-Reviewed Original ResearchConceptsMuscle specificationEpithelial sheath cellsMyoblast fusionSheath cellsProtein trapSarcomere organizationFLP/FRT systemMononuclear muscle cellsMuscle cellsDrosophila ovaryGonadal mesodermGenetic mosaicsKey genesTrap linesFRT systemGenetic analysisHuman muscle physiologySomatic musclesVisceral musclesSingle nucleusClonal analysisFemale reproductive systemMuscle physiologyEpithelial sheathModel systemUNDERSTANDING 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 characteristicsActinScreenUnderstandingOvariesA 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 requirements
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