Search results for "DROSOPHILA"

showing 10 items of 782 documents

The Drosophila Larval Locomotor Circuit Provides a Model to Understand Neural Circuit Development and Function

2021

It is difficult to answer important questions in neuroscience, such as: “how do neural circuits generate behaviour?,” because research is limited by the complexity and inaccessibility of the mammalian nervous system. Invertebrate model organisms offer simpler networks that are easier to manipulate. As a result, much of what we know about the development of neural circuits is derived from work in crustaceans, nematode worms and arguably most of all, the fruit fly, Drosophila melanogaster. This review aims to demonstrate the utility of the Drosophila larval locomotor network as a model circuit, to those who do not usually use the fly in their work. This utility is explored first by discussion…

0301 basic medicineComputer scienceCognitive Neurosciencemedia_common.quotation_subjectved/biology.organism_classification_rank.speciesNeuroscience (miscellaneous)Neurosciences. Biological psychiatry. Neuropsychiatry03 medical and health sciencesCellular and Molecular Neuroscience0302 clinical medicineDevelopment (topology)Biological neural networkModel organismFunction (engineering)DrosophilaElectronic circuitmedia_commonbiologyved/biologyvariabilityfungiconnectomebiology.organism_classificationSensory Systemscritical periodlocomotion030104 developmental biologyConnectomeDrosophilaDrosophila melanogasterNeurosciencecircuit030217 neurology & neurosurgeryRC321-571Frontiers in Neural Circuits
researchProduct

Loss of ISWI Function in Drosophila Nuclear Bodies Drives Cytoplasmic Redistribution of Drosophila TDP-43

2018

Over the past decade, evidence has identified a link between protein aggregation, RNA biology, and a subset of degenerative diseases. An important feature of these disorders is the cytoplasmic or nuclear aggregation of RNA-binding proteins (RBPs). Redistribution of RBPs, such as the human TAR DNA-binding 43 protein (TDP-43) from the nucleus to cytoplasmic inclusions is a pathological feature of several diseases. Indeed, sporadic and familial forms of amyotrophic lateral sclerosis (ALS) and fronto-temporal lobar degeneration share as hallmarks ubiquitin-positive inclusions. Recently, the wide spectrum of neurodegenerative diseases characterized by RBPs functions’ alteration and loss was coll…

0301 basic medicineCytoplasmCytoplasmic inclusionFluorescent Antibody TechniqueProtein aggregationHeterogeneous ribonucleoprotein particleHeterogeneous-Nuclear Ribonucleoproteinslcsh:Chemistry0302 clinical medicineDrosophila Proteinsneurodegenerative diseasesnuclear bodylcsh:QH301-705.5SpectroscopyGeneral MedicinehnRNPsComputer Science ApplicationsCell biologyChromatinTransport proteinDNA-Binding ProteinsProtein Transportmedicine.anatomical_structureDrosophilaDrosophila ProteinProtein BindingImitation SWIBiologyCatalysisArticleInorganic Chemistryomega speckles03 medical and health sciencesmedicineAnimalsPhysical and Theoretical ChemistryMolecular BiologyGenetic Association StudiesCell NucleusOrganic Chemistryta1182Chromatin Assembly and DisassemblyCell nucleus030104 developmental biologylcsh:Biology (General)lcsh:QD1-999gene expression<i>Drosophila</i>; nuclear body; omega speckles; dTDP-43; hnRNPs; omega speckles; neurodegenerative diseases; gene expression; gene regulationdTDP-43gene regulation030217 neurology & neurosurgeryInternational Journal of Molecular Sciences
researchProduct

Enterocyte Purge and Rapid Recovery Is a Resilience Reaction of the Gut Epithelium to Pore-Forming Toxin Attack.

2016

International audience; Besides digesting nutrients, the gut protects the host against invasion by pathogens. Enterocytes may be subjected to damage by both microbial and host defensive responses, causing their death. Here, we report a rapid epithelial response that alleviates infection stress and protects the enterocytes from the action of microbial virulence factors. Intestinal epithelia exposed to hemolysin, a pore-forming toxin secreted by Serratia marcescens, undergo an evolutionarily conserved process of thinning followed by the recovery of their initial thickness within a few hours. In response to hemolysin attack, Drosophila melanogaster enterocytes extrude most of their apical cyto…

0301 basic medicineCytoplasmDisease toleranceSurvivalApoptosismedicine.disease_causeOral infectionHemolysin ProteinsLipid droplet[SDV.IDA]Life Sciences [q-bio]/Food engineeringMitochondrial extrusionIntestinal MucosaSerratia marcescensBacterial-infectionPore-forming toxinbiologyCell DeathMicrovilliPlasma-membrane[ SDV.IDA ] Life Sciences [q-bio]/Food engineeringGut EpitheliumMitochondriamedicine.anatomical_structureDrosophila melanogasterEnterocyteVirulence FactorsVarroidaeSerratia-marcescensBacterial ToxinsVirulenceMicrobiologyMicrobiologySerratia Infections03 medical and health sciencesVirologymedicineAnimalsApical cytoplasmDefense strategyDrosophila cyclin jToxinbiology.organism_classificationLipid dropletsDisease Models AnimalIntestinal Diseases030104 developmental biologyEnterocytesSerratia marcescensParasitologyDigestive SystemCell hostmicrobe
researchProduct

GW-Bodies and P-Bodies Constitute Two Separate Pools of Sequestered Non-Translating RNAs

2015

Non-translating RNAs that have undergone active translational repression are culled from the cytoplasm into P-bodies for decapping-dependent decay or for sequestration. Organisms that use microRNA-mediated RNA silencing have an additional pathway to remove RNAs from active translation. Consequently, proteins that govern microRNA-mediated silencing, such as GW182/Gw and AGO1, are often associated with the P-bodies of higher eukaryotic organisms. Due to the presence of Gw, these structures have been referred to as GW-bodies. However, several reports have indicated that GW-bodies have different dynamics to P-bodies. Here, we use live imaging to examine GW-body and P-body dynamics in the early …

0301 basic medicineCytoplasmEmbryologyTranscription GeneticMolecular biologylcsh:MedicineGene ExpressionRNA-binding proteinsRNA-binding proteinBiochemistryBlastulas0302 clinical medicineRNA interferenceDrosophila ProteinsCell Cycle and Cell DivisionSmall nucleolar RNAlcsh:ScienceRNA structureGeneticsMultidisciplinaryDrosophila MelanogasterAnimal ModelsArgonauteLong non-coding RNACell biologyInsectsNucleic acidsRNA silencingCell ProcessesArgonaute ProteinsRNA InterferenceRNA Long NoncodingDrosophilaCellular Structures and OrganellesResearch ArticleArthropodaBiologyResearch and Analysis Methods03 medical and health sciencesModel OrganismsP-bodiesGeneticsAnimalsBlastodermlcsh:REmbryosOrganismsBiology and Life SciencesProteinsRNACell BiologyInvertebratesMicroRNAsMacromolecular structure analysis030104 developmental biologyProtein BiosynthesisRNAlcsh:QProtein Translation030217 neurology & neurosurgeryDevelopmental BiologyPLOS ONE
researchProduct

Modeling of Myotonic Dystrophy Cardiac Phenotypes in Drosophila

2018

After respiratory distress, cardiac dysfunction is the second most common cause of fatality associated with the myotonic dystrophy (DM) disease. Despite the prevalance of heart failure in DM, physiopathological studies on heart symptoms have been relatively scarce because few murine models faithfully reproduce the cardiac disease. Consequently, only a small number of candidate compounds have been evaluated in this specific phenotype. To help cover this gap Drosophila combines the amenability of its invertebrate genetics with the possibility of quickly acquiring physiological parameters suitable for meaningful comparisons with vertebrate animal models and humans. Here we review available des…

0301 basic medicineDaunorubicinDiseaseBioinformaticsMyotonic dystrophyMuscleblindlcsh:RC346-42903 medical and health sciencesCTG expansionmedicineDrosophilalcsh:Neurology. Diseases of the nervous systemmyotonic dystrophybiologyRespiratory distresscardiac dysfunctionCCTG expansionRNADrosophila disease modelbiology.organism_classificationmedicine.diseasePhenotype030104 developmental biologyNeurologyHeart failureNeurology (clinical)medicine.drugFrontiers in Neurology
researchProduct

Intra-neuronal Competition for Synaptic Partners Conserves the Amount of Dendritic Building Material

2017

Brain development requires correct targeting of multiple thousand synaptic terminals onto staggeringly complex dendritic arbors. The mechanisms by which input synapse numbers are matched to dendrite size, and by which synaptic inputs from different transmitter systems are correctly partitioned onto a postsynaptic arbor, are incompletely understood. By combining quantitative neuroanatomy with targeted genetic manipulation of synaptic input to an identified Drosophila neuron, we show that synaptic inputs of two different transmitter classes locally direct dendrite growth in a competitive manner. During development, the relative amounts of GABAergic and cholinergic synaptic drive shift dendrit…

0301 basic medicineDendritic spinePresynaptic TerminalsBiologyReceptors NicotinicArticleSynapse03 medical and health sciencesDendrite (crystal)Calcium Channels T-Type0302 clinical medicinePostsynaptic potentialSynaptic augmentationmedicineAnimalsDrosophila ProteinsCalcium Signalinggamma-Aminobutyric AcidNeuronsNeuronal PlasticityGeneral NeuroscienceDendritesReceptors GABA-AAcetylcholine030104 developmental biologySynaptic fatiguemedicine.anatomical_structurenervous systemSynaptic plasticitySynapsesDrosophilaNeuronNeuroscience030217 neurology & neurosurgery
researchProduct

Retinal homeobox promotes cell growth, proliferation and survival of mushroom body neuroblasts in the Drosophila brain.

2016

Abstract The Drosophila mushroom bodies, centers of olfactory learning and memory in the fly ‘forebrain’, develop from a set of neural stem cells (neuroblasts) that generate a large number of Kenyon cells (KCs) during sustained cell divisions from embryonic to late pupal stage. We show that retinal homeobox ( rx ), encoding for an evolutionarily conserved transcription factor, is required for proper development of the mushroom bodies. Throughout development rx is expressed in mushroom body neuroblasts (MBNBs), their ganglion mother cells (MB-GMCs) and young KCs. In the absence of rx function, MBNBs form correctly but exhibit a reduction in cell size and mitotic activity, whereas overexpress…

0301 basic medicineEmbryologyanimal structuresNerve Tissue ProteinsBiologyRetina03 medical and health sciencesNeuroblastNeural Stem CellsAnimalsDrosophila ProteinsMitosisMushroom BodiesCell ProliferationGanglion CystsHomeodomain ProteinsNeuronsCell growthfungiCell CycleBrainNuclear ProteinsAnatomyEmbryonic stem cellNeural stem cellCell biologyRepressor Proteins030104 developmental biologyDrosophila melanogasterLarvaMushroom bodiesForebrainHomeoboxDevelopmental BiologyTranscription FactorsMechanisms of development
researchProduct

Rabphilin involvement in filtration and molecular uptake in Drosophila nephrocytes suggests a similar role in human podocytes

2020

ABSTRACT Drosophila nephrocytes share functional, structural and molecular similarities with human podocytes. It is known that podocytes express the rabphilin 3A (RPH3A)-RAB3A complex, and its expression is altered in mouse and human proteinuric disease. Furthermore, we previously identified a polymorphism that suggested a role for RPH3A protein in the development of urinary albumin excretion. As endocytosis and vesicle trafficking are fundamental pathways for nephrocytes, the objective of this study was to assess the role of the RPH3A orthologue in Drosophila, Rabphilin (Rph), in the structure and function of nephrocytes. We confirmed that Rph is required for the correct function of the en…

0301 basic medicineEndocytic cycle030232 urology & nephrologyRetinoic acidlcsh:MedicineMedicine (miscellaneous)Labyrinthine channelschemistry.chemical_compound0302 clinical medicineImmunology and Microbiology (miscellaneous)Chronic kidney diseaseDrosophila ProteinsSlit diaphragmGene knockdownPodocytesIntracellular Signaling Peptides and ProteinsDrosophila nephrocyteEndocytosisCell biologyProtein TransportDrosophila melanogasterLarvaSlit diaphragmFemaleRNA InterferenceEndocytic pathwaylcsh:RB1-214Research ArticleEndosomeNeuroscience (miscellaneous)Nerve Tissue ProteinsTretinoinCell fate determinationBiologyEndocytosisGeneral Biochemistry Genetics and Molecular Biology03 medical and health scienceslcsh:PathologyRabphilinAnimalsHumansCell Lineagelcsh:RCytoplasmic VesiclesDrosCubilinSurvival Analysis030104 developmental biologychemistrySilver NitrateDisease Models &amp; Mechanisms
researchProduct

Adaptation of gene loci to heterochromatin in the course of Drosophila evolution is associated with insulator proteins.

2020

AbstractPericentromeric heterochromatin is generally composed of repetitive DNA forming a transcriptionally repressive environment. Dozens of genes were embedded into pericentromeric heterochromatin during evolution of Drosophilidae lineage while retaining activity. However, factors that contribute to insusceptibility of gene loci to transcriptional silencing remain unknown. Here, we find that the promoter region of genes that can be embedded in both euchromatin and heterochromatin exhibits a conserved structure throughout the Drosophila phylogeny and carries motifs for binding of certain chromatin remodeling factors, including insulator proteins. Using ChIP-seq data, we demonstrate that ev…

0301 basic medicineEuchromatinHeterochromatinEvolutionMolecular biologyAdaptation Biologicallcsh:MedicineInsulator (genetics)Chromatin remodelingArticleEvolutionary geneticsEvolution Molecular03 medical and health sciences0302 clinical medicineDrosophilidaeHeterochromatinAnimalsDrosophila ProteinsNucleotide Motifslcsh:ScienceEye ProteinsPromoter Regions GeneticGenePericentric heterochromatinPhylogenyGeneticsMultidisciplinarygeenitBinding Sitesbiologylcsh:RfungiChromosome MappingPromoterDNAbiology.organism_classificationChromatinDNA-Binding Proteins030104 developmental biologyGene Expression RegulationGenetic LociChromatin Immunoprecipitation SequencingMolecular evolutionlcsh:QDrosophilaTranscription Initiation SiteTranscription030217 neurology & neurosurgeryProtein BindingScientific reports
researchProduct

Evolutionary conserved role of eukaryotic translation factor eIF5A in the regulation of actin-nucleating formins

2017

AbstractElongation factor eIF5A is required for the translation of consecutive prolines, and was shown in yeast to translate polyproline-containing Bni1, an actin-nucleating formin required for polarized growth during mating. Here we show that Drosophila eIF5A can functionally replace yeast eIF5A and is required for actin-rich cable assembly during embryonic dorsal closure (DC). Furthermore, Diaphanous, the formin involved in actin dynamics during DC, is regulated by and mediates eIF5A effects. Finally, eIF5A controls cell migration and regulates Diaphanous levels also in mammalian cells. Our results uncover an evolutionary conserved role of eIF5A regulating cytoskeleton-dependent processes…

0301 basic medicineFluorescent Antibody Techniquelcsh:Medicinemacromolecular substancesBiologyArticleMiceEukaryotic cells03 medical and health sciencesEukaryotic translationCell MovementPeptide Initiation FactorsCitosqueletProtein biosynthesisAnimalsProtein Interaction Domains and Motifslcsh:ScienceCytoskeletonActinMultidisciplinaryCèl·lules eucariotesMicrofilament Proteinsfungilcsh:RGene Expression Regulation DevelopmentalRNA-Binding ProteinsTranslation (biology)Biological EvolutionActinsDorsal closureCell biologyElongation factor030104 developmental biologyProtein BiosynthesisForminsMutationbiology.proteinDrosophilalcsh:QEIF5AScientific Reports
researchProduct