Featured Publications
Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion
Hudson AM, Mannix KM, Gerdes JA, Kottemann MC, Cooley L. Targeted substrate degradation by Kelch controls the actin cytoskeleton during ring canal expansion. Development 2018, 146: dev169219. PMID: 30559276, PMCID: PMC6340150, DOI: 10.1242/dev.169219.Peer-Reviewed Original ResearchConceptsTandem affinity purificationUbiquitin ligase complexCullin-3 functionShort sequence motifsSpecialized cytoskeletal structuresUbiquitin-proteasome systemF-actin cytoskeletonSpecialized actinLigase complexActin cytoskeletonRing canalsSequence motifsGenetic evidenceCytoskeletal structuresAffinity purificationCytoskeletonSubstrate degradationBiochemical evidenceUnusual mechanismKelchCRL3CullinMass spectrometryOogenesisMutagenesisActin 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-actinCytoskeletonLigaseProteasomeVivoCul3MutagenesisDrosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton
Hudson AM, Cooley L. Drosophila Kelch functions with Cullin-3 to organize the ring canal actin cytoskeleton. Journal Of Cell Biology 2010, 188: 29-37. PMID: 20065088, PMCID: PMC2812842, DOI: 10.1083/jcb.200909017.Peer-Reviewed Original ResearchConceptsDrosophila KelchCullin 3Cullin-RING ubiquitin E3 ligasesGermline ring canalsSubstrate adaptor proteinCullin-RING ligaseDiverse protein familiesF-actin cytoskeletal structureUbiquitin E3 ligasesProtein ubiquitylationActin cytoskeletonE3 ligasesRing canalsAdaptor proteinProtein familySequence motifsCytoskeletal structuresFilamentous actinKelchProteinUbiquitylationLigasesCytoskeletonLigaseRepeatsPhylogenetic, 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 ResearchConceptsΒ-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
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
1997
Formation 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