Andrew Hudson, PhD
Senior Research Scientist in GeneticsCards
About
Research
Publications
Featured Publications
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 cellsDrosophilaTargeted 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-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 systemDrosophila 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 relationshipFamilySuperfamilyAncestorUNDERSTANDING 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 characteristicsActinScreenUnderstandingOvariesArp2/3-Dependent Psuedocleavage Furrow Assembly in Syncytial Drosophila Embryos
Stevenson V, Hudson A, Cooley L, Theurkauf WE. Arp2/3-Dependent Psuedocleavage Furrow Assembly in Syncytial Drosophila Embryos. Current Biology 2002, 12: 705-711. PMID: 12007413, DOI: 10.1016/s0960-9822(02)00807-2.Peer-Reviewed Original ResearchConceptsDrosophila embryosPseudocleavage furrowsCell cycleActin capActin reorganizationSomatic cell divisionLocal actin polymerizationSyncytial Drosophila embryosARPC1 subunitArp2/3 complexNuclear positioningEmbryonic divisionsComplex localizeCell divisionActin polymerizationCleavage furrowFurrow formationCap functionSpindle fusionMolecular mechanismsArp2/3EmbryosVivo analysisMutationsAssemblyA 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 cytoplasmSubunitsMutationsComplexes