Featured Publications
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 relationshipFamilySuperfamilyAncestorA 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