Search results for "La Protein"

showing 10 items of 245 documents

Connecting temporal identity to mitosis: the regulation of Hunchback in Drosophila neuroblast lineages.

2006

Both in vertebrates and invertebrates, neural stem cells generate different cell types at different times during development. It has been suggested that this process depends on temporal identity transitions of neural progenitors, but the underlying mechanism has not been resolved, yet. Recently, Drosophila neuroblasts (NBs) have been shown to be an excellent model system to investigate this subject. Here, changes in temporal identity are regulated by sequential and transient expression of transcription factors in the NB, such as Hunchback (Hb) and Kruppel (Kr). The temporal expression profile is maintained in the progeny. Hb is expressed first and thus defines the earliest identity in a giv…

Retinal Ganglion CellsCell typeReceptors SteroidKruppel-Like Transcription FactorsDown-RegulationMitosisNerve Tissue ProteinsBiologyCell fate determinationKrüppelNeuroblastAnimalsDrosophila ProteinsNuclear export signalMolecular BiologyMitosisTranscription factorGeneticsNeuronsModels GeneticNuclear ProteinsCell DifferentiationCell BiologyNeural stem cellDNA-Binding ProteinsProtein BiosynthesisDrosophilaDevelopmental BiologyTranscription FactorsCell cycle (Georgetown, Tex.)
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The GTP- and Phospholipid-Binding Protein TTD14 Regulates Trafficking of the TRPL Ion Channel in Drosophila Photoreceptor Cells

2015

Recycling of signaling proteins is a common phenomenon in diverse signaling pathways. In photoreceptors of Drosophila, light absorption by rhodopsin triggers a phospholipase Cβ-mediated opening of the ion channels transient receptor potential (TRP) and TRP-like (TRPL) and generates the visual response. The signaling proteins are located in a plasma membrane compartment called rhabdomere. The major rhodopsin (Rh1) and TRP are predominantly localized in the rhabdomere in light and darkness. In contrast, TRPL translocates between the rhabdomeral plasma membrane in the dark and a storage compartment in the cell body in the light, from where it can be recycled to the plasma membrane upon subsequ…

RhodopsinCancer Researchlcsh:QH426-470LightGTP'BiologyEye03 medical and health sciencesTransient receptor potential channelTransient Receptor Potential Channels0302 clinical medicineGTP-binding protein regulatorsGTP-Binding ProteinsGeneticsAnimalsDrosophila ProteinsMolecular BiologyGenetics (clinical)Ecology Evolution Behavior and SystematicsIon channel030304 developmental biology0303 health sciencesCell MembraneMembrane ProteinsDarknessRhabdomereTransport proteinCell biologylcsh:GeneticsProtein TransportDrosophila melanogasterMembrane proteinRhodopsinMutationbiology.proteinPhotoreceptor Cells Invertebrate030217 neurology & neurosurgerySignal TransductionResearch ArticlePLOS Genetics
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Chromatin-associated RNA interference components contribute to transcriptional regulation in Drosophila

2009

RNA interference (RNAi) pathways have evolved as important modulators of gene expression that operate in the cytoplasm by degrading RNA target molecules through the activity of short (21-30 nucleotide) RNAs1-6. RNAi components have been reported to have a role in the nucleus, as they are involved in epigenetic regulation and heterochromatin formation(7-10). However, although RNAi-mediated post-transcriptional gene silencing is well documented, the mechanisms of RNAi-mediated transcriptional gene silencing and, in particular, the role of RNAi components in chromatin dynamics, especially in animal multicellular organisms, are elusive. Here we show that the key RNAi components Dicer 2 (DCR2) a…

Ribonuclease IIIanimal structuresRNA-induced transcriptional silencingTranscription GeneticRNA-induced silencing complexBiology03 medical and health sciences0302 clinical medicineRNA interferenceTranscriptional regulationAnimalsDrosophila ProteinsHSP70 Heat-Shock ProteinsPromoter Regions Genetic030304 developmental biologyRNA Double-StrandedGenetics0303 health sciencesMultidisciplinaryfungiRNARNA-Binding ProteinsChromatinChromatinRNA silencingMicroRNAsDrosophila melanogasterGene Expression RegulationArgonaute ProteinsRNA InterferenceRNA Polymerase II030217 neurology & neurosurgeryDrosophila ProteinHeat-Shock ResponseRNA HelicasesProtein BindingTranscription Factors
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The human protein Hugl-1 substitutes for Drosophila lethal giant larvae tumour suppressor function in vivo

2004

Drosophila lethal giant larvae: (lgl), discs large (dlg) and scribble (scrib) are tumour suppressor genes acting in a common pathway, whose loss of function leads to disruption of cell polarity and tissue architecture, uncontrolled proliferation and growth of neoplastic lesions. Mammalian homologues of these genes are highly conserved and evidence is emerging concerning their role in cell proliferation control and tumorigenesis in humans. Here we investigate the functional conservation between Drosophila lethal giant larvae and its human homologue Hugl-1(Llgl1). We first show that Hugl-1 is lost in human solid malignancies, supporting its role as a tumour suppressor in humans. Hugl-1 expres…

SCRIBCancer ResearchTumor suppressor geneBiologymedicine.disease_causeEyelaw.inventionlawDrosophilidaeCell polarityGeneticsmedicineAnimalsDrosophila ProteinsHumansRNA MessengerMolecular BiologyGeneticsCell growthTumor Suppressor ProteinsfungiCell polarity; Drosophila; Epithelial cancers; Hugl-1; Lethal giant larvae; Tumour suppressorGene Expression Regulation DevelopmentalMembrane ProteinsProteinsHugl-1Lethal giant larvaebiology.organism_classificationCell biologyCytoskeletal ProteinsLarvaCell polaritySuppressorDrosophilaDrosophila melanogasterEpithelial cancersCarcinogenesisTumour suppressorProtein Binding
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Serum Response Factor-Mediated Gene Regulation in a Drosophila Visual Working Memory

2013

Summary Background Navigation through the environment requires a working memory for the chosen target and path integration facilitating an approach when the target becomes temporarily hidden. We have previously shown that this visual orientation memory resides in the ellipsoid body, which is part of the central complex in the Drosophila brain. Former analysis of  foraging and ignorant mutants have revealed that a hierarchical PKG and RSKII kinase signaling cascade in a subset of the ellipsoid-body ring neurons is required for this type of working memory in flies. Results Here we show that mutants in the ellipsoid body open  ( ebo ) gene, which encodes the actin-binding protein Exportin 6, e…

Serum Response FactorMutantKaryopherinsBiologyGeneral Biochemistry Genetics and Molecular Biology03 medical and health sciences0302 clinical medicineOrientationCoactivatorSerum response factorNeuropilmedicineAnimalsDrosophila ProteinsTranscription factor030304 developmental biologyCell NucleusGeneticsRegulation of gene expression0303 health sciencesModels GeneticAgricultural and Biological Sciences(all)Biochemistry Genetics and Molecular Biology(all)Working memoryMicrofilament ProteinsfungiLong-term potentiationActinsCell biologyDrosophila melanogasterMemory Short-Termmedicine.anatomical_structureGene Expression RegulationMutationVisual PerceptionGeneral Agricultural and Biological Sciences030217 neurology & neurosurgeryCurrent Biology
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Functional antagonism between histone H3K4 demethylases in vivo

2011

Dynamic regulation of histone modifications is critical during development, and aberrant activity of chromatin-modifying enzymes has been associated with diseases such as cancer. Histone demethylases have been shown to play a key role in eukaryotic gene transcription; however, little is known about how their activities are coordinated in vivo to regulate specific biological processes. In Drosophila, two enzymes, dLsd1 (Drosophila ortholog of lysine-specific demethylase 1) and Lid (little imaginal discs), demethylate histone H3 at Lys 4 (H3K4), a residue whose methylation is associated with actively transcribed genes. Our studies show that compound mutation of Lid and dLsd1 results in increa…

Settore BIO/11 - Biologia MolecolareBiologyMethylationHistoneshistone demethylasesHistone H3HeterochromatinHistone H2AHistone methylationGeneticsAnimalsDrosophila ProteinsHistone codeGeneticsReceptors NotchEZH2Oxidoreductases N-DemethylatingHistone-Lysine N-MethyltransferaseSettore BIO/18 - GeneticaDrosophila melanogasterPhenotypeGene Expression RegulationHistone methyltransferaseMutationHeterochromatin protein 1Histone DemethylasesSignal TransductionResearch PaperDevelopmental Biology
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dfh is a Drosophila homolog of the Friedreich's ataxia disease gene

2000

Abstract A putative Drosophila homolog of the Friedreich's ataxia disease gene (FRDA) has been cloned and characterized; it has been named Drosophila frataxin homolog (dfh). It is located at 8C/D position on X chromosome and is spread over 1 kb, a much smaller genomic region than the human gene. Its genomic organization is simple, with a single intron dividing the coding region into two exons. The predicted encoded product has 190 amino acids, being considered a frataxin-like protein on the basis of the sequence and secondary structure conservation when compared with human frataxin and related proteins from other eukaryotes. The closest match between the Drosophila and the human proteins in…

Signal peptideDNA ComplementaryEmbryo NonmammalianMolecular Sequence DataMutantEmbryonic DevelopmentGenes InsectExonIron-Binding ProteinsGeneticsAnimalsDrosophila ProteinsCoding regionAmino Acid SequenceRNA MessengerCloning MolecularGeneIn Situ HybridizationGenomic organizationGeneticsSequence Homology Amino AcidbiologyIntronGene Expression Regulation DevelopmentalDNAExonsSequence Analysis DNAGeneral MedicineBlotting NorthernIntronsPhosphotransferases (Alcohol Group Acceptor)Drosophila melanogasterFriedreich AtaxiaFrataxinbiology.proteinDrosophilaSequence AlignmentGene
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Sequence of the new Drosophila melanogaster small heat-shock-related gene, lethal(2) essential for life [l(2)efl], at locus 59F4,5.

1995

Abstract In this study, we report the molecular cloning of a novel Drosophila melanogaster small heat-shock (HS)-homologous gene, l(2)efl, identified on the right arm of the second chromosome at locus 59F4,5. We describe the temporal expression of l(2)efl in the wild-type and present its structure. The deduced amino-acid sequence of the Efl protein shows significant homology to all known small HS proteins identified in Drosophila and vertebrates, and to mammalian α-crystallin.

Signal peptideTranscription GeneticMolecular Sequence DataRestriction MappingLocus (genetics)Genes InsectMolecular cloningHomology (biology)biology.animalSequence Homology Nucleic AcidGeneticsAnimalsDrosophila ProteinsAmino Acid SequenceRNA MessengerRelated geneCloning MolecularGeneHeat-Shock ProteinsIn Situ HybridizationGeneticsbiologyBase SequenceSequence Homology Amino AcidVertebrateGeneral MedicineSequence Analysis DNAbiology.organism_classificationDrosophila melanogasterInsect HormonesGenes LethalDrosophila melanogasterGene
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Cloning and characterization of the promoter of Hugl-2, the human homologue of Drosophila lethal giant larvae (lgl) polarity gene.

2007

The human lgl gene, Hugl-2 (llgl2, Lgl2), codes for a cytoskeletal protein involved in regulating cell polarity. Here, we report the identification and functional characterization of the promoter region ( approximately 1.2kb) of the Hugl-2 gene. Luciferase expression assays show a high basal Hugl-2 promoter activity in different cell lines and primary human hepatocytes. Truncations of the promoter identified a GC-rich region important for this activity. Alignment of human and mouse genomic sequences demonstrate that this is an evolutionary conserved region fcontaining putative binding sites for several transcription factors including Elk-1 and Sp-1. Mithramycin A reduces Hugl-2 expression i…

Sp1 Transcription FactorMolecular Sequence DataBiophysicsDown-RegulationGenes InsectBiologyBiochemistryCell LineDownregulation and upregulationEpidermal growth factorCell polarityChlorocebus aethiopsAnimalsDrosophila ProteinsHumansLuciferaseCloning MolecularPromoter Regions GeneticMolecular BiologyGeneTranscription factorBase PairingBase SequenceEpidermal Growth FactorSequence Homology Amino AcidTumor Suppressor ProteinsCell PolarityPromoterCell BiologyMolecular biologyCytoskeletal ProteinsDrosophila melanogasterCell cultureCOS CellsSequence AlignmentBiochemical and biophysical research communications
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NineTeen Complex-subunit Salsa is required for efficient splicing of a subset of introns and dorsal-ventral patterning

2020

© 2020 Rathore et al. This article is distributed exclusively by the RNASociety for the first 12 months after the full-issue publication date (see http://rnajournal.cshlp.org/site/misc/terms.xhtml). After 12 months, it is available under a Creative Commons License (Attribution-NonCommercial 4.0 International), as described at http://creativecommons.org/licenses/by-nc/4.0/.

SpliceosomeBiochemistry & Molecular BiologyRNA SplicingBiologySplicingGermlineArticleMidblastulaDorsal-ventral patterning03 medical and health sciencesAnimalsDrosophila ProteinsFemale fertilityGurkenMolecular BiologyGene030304 developmental biologyBody Patterning0303 health sciencesMessenger RNA030302 biochemistry & molecular biologyfungiIntronGene Expression Regulation DevelopmentalTransforming Growth Factor alphaRNA Helicase AIntronsCell biologyDorsal-ventral patterning; Drosophila; Female fertility; Gurken; Splicing; dorsal–ventral patterning; female fertility; splicingDNA-Binding ProteinsDrosophila melanogasterRNA splicingSpliceosomesFemaleDrosophilaInfertility Female
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