Andrew Hudson, PhD
Senior Research Scientist in GeneticsCards
About
Research
Publications
2020
HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis
Gerdes JA, Mannix KM, Hudson AM, Cooley L. HtsRC-Mediated Accumulation of F-Actin Regulates Ring Canal Size During Drosophila melanogaster Oogenesis. Genetics 2020, 216: 717-734. PMID: 32883702, PMCID: PMC7648574, DOI: 10.1534/genetics.120.303629.Peer-Reviewed Original ResearchConceptsGermline ring canalsRing canalsActin cytoskeletonF-actinDrosophila melanogaster oogenesisSomatic follicle cellsCombination of CRISPRF-actin accumulationF-actin recruitmentFilamentous actin cytoskeletonFemale germlineActin structuresFruit flyHigh fecundityFollicle cellsCytoskeletonGermlineOverexpressionAccumulationDrosophilaOogenesisMutagenesisCRISPRFilaminGenes
2017
Remodeling the Actin Cytoskeleton by Ubiquitin‐Dependent Proteolysis
Mannix K, Gerdes J, Hudson A, Kaufman R, Cooley L. Remodeling the Actin Cytoskeleton by Ubiquitin‐Dependent Proteolysis. The FASEB Journal 2017, 31 DOI: 10.1096/fasebj.31.1_supplement.916.10.Peer-Reviewed Original Research
2014
Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers
Burn KM, Shimada Y, Ayers K, Vemuganti S, Lu F, Hudson A, Cooley L. Somatic insulin signaling regulates a germline starvation response in Drosophila egg chambers. Developmental Biology 2014, 398: 206-217. PMID: 25481758, PMCID: PMC4340711, DOI: 10.1016/j.ydbio.2014.11.021.Peer-Reviewed Original ResearchConceptsDrosophila insulin-like peptidesEgg chambersStarvation responseBody organizationDrosophila egg chamberMotor protein dyneinNutrient-rich conditionsPoor nutrient availabilityInsulin-like peptidesProcessing bodiesDrosophila femalesGermline cellsP-bodiesNutrient availabilityDynein activityInsulin signalingProgeny survivalInsulin pathwayKinesin activityFollicle cellsMicrotubulesStarvationBovine insulinPotential mechanismsProtective response
2012
Expression of Ixodes scapularis Antifreeze Glycoprotein Enhances Cold Tolerance in Drosophila melanogaster
Neelakanta G, Hudson AM, Sultana H, Cooley L, Fikrig E. Expression of Ixodes scapularis Antifreeze Glycoprotein Enhances Cold Tolerance in Drosophila melanogaster. PLOS ONE 2012, 7: e33447. PMID: 22428051, PMCID: PMC3302814, DOI: 10.1371/journal.pone.0033447.Peer-Reviewed Original ResearchMeSH KeywordsAcclimatizationAnalysis of VarianceAnimalsAnimals, Genetically ModifiedAntifreeze ProteinsApoptosisCold TemperatureDrosophila melanogasterEmbryo, NonmammalianEnzyme-Linked Immunosorbent AssayFemaleImmunoblottingIn Situ Nick-End LabelingIxodesMaleMusclesOligonucleotidesReal-Time Polymerase Chain ReactionConceptsNon-freezing temperaturesD. melanogasterDrosophila melanogasterCold toleranceLow non-freezing temperaturesFemale adult fliesTransgenic D. melanogasterCold shock injuryAbility of fliesAntifreeze glycoproteinsAdult fliesMolecular basisMelanogasterFlight musclesFliesAntifreeze proteinsHatching rateHigher survival rateApoptotic damageGlycoproteinExpressionToleranceEmbryosProteinApoptosis
2007
Exploring Strategies for Protein Trapping in Drosophila
Quiñones-Coello A, Petrella LN, Ayers K, Melillo A, Mazzalupo S, Hudson AM, Wang S, Castiblanco C, Buszczak M, Hoskins RA, Cooley L. Exploring Strategies for Protein Trapping in Drosophila. Genetics 2007, 175: 1089-1104. PMID: 17179094, PMCID: PMC1840052, DOI: 10.1534/genetics.106.065995.Peer-Reviewed Original ResearchConceptsGreen fluorescent proteinProtein trapEnhancer trapFluorescent proteinExpression dataGFP expressionGFP fusion proteinFluorescent protein tagsCell biological studiesProduction of GFPWeb-accessible databaseChromosomal positionProtein tagsProtein trappingEndogenous proteinsGenomic DNASplice acceptorDonor sequenceNew insertionsMolecular informationGenesProteinDrosophilaTransposonBiological studies
2002
Arp2/3-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 analysisMutationsAssemblySCAR 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 requirementsDrosophila 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