Search results for "G proteins"

showing 10 items of 992 documents

Phylointeractomics reconstructs functional evolution of protein binding

2017

Molecular phylogenomics investigates evolutionary relationships based on genomic data. However, despite genomic sequence conservation, changes in protein interactions can occur relatively rapidly and may cause strong functional diversification. To investigate such functional evolution, we here combine phylogenomics with interaction proteomics. We develop this concept by investigating the molecular evolution of the shelterin complex, which protects telomeres, across 16 vertebrate species from zebrafish to humans covering 450 million years of evolution. Our phylointeractomics screen discovers previously unknown telomere-associated proteins and reveals how homologous proteins undergo functiona…

Proteomics0301 basic medicineLineage (evolution)ScienceTelomere-Binding ProteinsGeneral Physics and AstronomyGenomicsBiologyProteomicsArticleGeneral Biochemistry Genetics and Molecular BiologyConserved sequenceEvolution Molecular03 medical and health sciencesPhylogeneticsMolecular evolutionPhylogenomicsAnimalsCells CulturedConserved SequencePhylogenyGeneticsGenomeMultidisciplinaryQComputational BiologyGenomicsSequence Analysis DNAGeneral ChemistryTelomereProtein superfamily030104 developmental biologyEvolutionary biologyVertebratesSequence AlignmentProtein Binding
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SANS (USH1G) regulates pre-mRNA splicing by mediating the intra-nuclear transfer of tri-snRNP complexes

2021

Abstract Splicing is catalyzed by the spliceosome, a compositionally dynamic complex assembled stepwise on pre-mRNA. We reveal links between splicing machinery components and the intrinsically disordered ciliopathy protein SANS. Pathogenic mutations in SANS/USH1G lead to Usher syndrome—the most common cause of deaf-blindness. Previously, SANS was shown to function only in the cytosol and primary cilia. Here, we have uncovered molecular links between SANS and pre-mRNA splicing catalyzed by the spliceosome in the nucleus. We show that SANS is found in Cajal bodies and nuclear speckles, where it interacts with components of spliceosomal sub-complexes such as SF3B1 and the large splicing cofact…

ProteomicsAcademicSubjects/SCI00010Ribonucleoprotein U4-U6 Small NuclearSF3B1 GeneMass Spectrometry0302 clinical medicineRNA Small NuclearRNA PrecursorsIn Situ Hybridization FluorescenceRibonucleoprotein0303 health sciencesChemistryRibonucleoproteins Small NuclearImmunohistochemistryCell biologyDNA-Binding Proteinsmedicine.anatomical_structureGene Knockdown TechniquesRNA splicingRNA Splicing FactorsUsher SyndromesSpliceosomeCoiled BodiesNerve Tissue ProteinsBiologyMinor Histocompatibility Antigens03 medical and health sciencesMicroscopy Electron TransmissionRNA and RNA-protein complexesGeneticsmedicineHumanssnRNPEye ProteinsGeneCell Proliferation030304 developmental biologyCell NucleusRNAmedicine.diseasePhosphoproteinsCiliopathyAlternative SplicingCell nucleusHEK293 CellsCajal bodyCytoplasmSpliceosomesNucleus030217 neurology & neurosurgeryTranscription FactorsNucleic Acids Research
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Nacre calcification in the freshwater mussel Unio pictorum: carbonic anhydrase activity and purification of a 95 kDa calcium-binding glycoprotein.

2008

9 pages; International audience; The formation of the molluscan shell is finely tuned by macromolecules of the shell organic matrix. Previous results have shown that the acid-soluble fraction of the nacre matrix of the freshwater paleoheterodont bivalve Unio pictorum shell displays a number of remarkable properties, such as calcium-binding activity, the presence of extensive glycosylations and the capacity to interfere at low concentration with in vitro calcium carbonate precipitation. Here we have found that the nacre-soluble matrix exhibits a carbonic anhydrase activity, an important function in calcification processes. This matrix is composed of three main proteinaceous discrete fraction…

ProteomicsCarbonateschemistry.chemical_elementFresh WaterCalciumBiochemistryMass Spectrometry03 medical and health scienceschemistry.chemical_compoundCalcification PhysiologicCalcium-binding proteinCarbonic anhydraseMollusc shellmedicineAnimalsGlycosyl[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyAmino Acid Sequence[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsMolecular Biology[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyCarbonic AnhydrasesGlycoproteins030304 developmental biologychemistry.chemical_classificationbiomineralization; mollusc shell nacre; carbonic anhydrase; 2-DE; two-dimensional electrophoresis; organic matrix0303 health sciencesbiologyCalcium-Binding Proteins030302 biochemistry & molecular biologyOrganic ChemistryUnio pictorumbiology.organism_classificationTrypsin[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/BiomaterialsBivalviaEnzyme ActivationMolecular WeightSolubilitychemistryBiochemistryMicroscopy Electron Scanningbiology.proteinMolecular MedicineCalciumGlycoproteinGelsSequence Analysismedicine.drug
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Changes in the proteome of sea urchin Paracentrotus lividus coelomocytes in response to LPS injection into the body cavity.

2020

Background The immune system of echinoderm sea urchins is characterised by a high degree of complexity that is not completely understood. The Mediterranean sea urchin Paracentrotus lividus coelomocytes mediate immune responses through phagocytosis, encapsulation of non-self particles, and production of diffusible factors including antimicrobial molecules. Details of these processes, and molecular pathways driving these mechanisms, are still to be fully elucidated. Principal findings In the present study we treated the sea urchin P. lividus with the bacterial lipopolysaccharide (LPS) and collected coelomocytes at different time-points (1, 3, 6 and 24 hours). We have shown, using label-free q…

ProteomicsLipopolysaccharidesProteomeHydrolasesBiochemistry0302 clinical medicineParacentrotusMedicine and Health SciencesSea urchinCoelomocyteImmune ResponseCytoskeleton0303 health sciencesPhagocytesMultidisciplinarybiologyChemistryQREukaryotaAnimal ModelsCell biologyEnzymesEchinodermExperimental Organism Systems030220 oncology & carcinogenesisProteomeParacentrotusMedicineProtein Interaction NetworksCellular Structures and OrganellesNetwork AnalysisResearch ArticleEchinodermsComputer and Information Sciencesfood.ingredientScienceImmunologyLipopolysaccharideEndocytosisResearch and Analysis MethodsParacentrotus lividusLymphatic System03 medical and health sciencesfoodPhagocytosisbiology.animalHeat shock proteinDNA-binding proteinsAnimalsProtein Interactions030304 developmental biologyPhagocytosiAnimalOrganismsBiology and Life SciencesProteinsCell Biologybiology.organism_classificationInvertebratesCytoskeletal ProteinsGuanosine TriphosphataseProtein-Protein InteractionsPhagocyteImmune SystemSea UrchinsAnimal StudiesEnzymologyParacentrotuPLoS ONE
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Chronological expression of Ciliated Bronchial Epithelium 1 during pulmonary development

2009

Ciliated Bronchial Epithelium (CBE) 1 is a novel gene, which is expressed in ciliated cells. As cilia are important during embryogenesis, the present authors characterised the murine homologue of CBE1 (Cbe1) and compared its temporal expression during murine and human lung development. Cbe1 cDNA was cloned and characterised using sequencing, standard PCR and Western blotting. Mouse and human embryonic/fetal lungs (HELs) were harvested for mRNA analysis and protein localisation in vivo and in vitro using RT-PCR and immunohistochemistry. The Cbe1 amino acid sequence was >75% identical with CBE1 and its alternative splicing and tissue distribution were highly conserved. Pulmonary expression of…

Pulmonary and Respiratory MedicinePathologymedicine.medical_specialtyDNA ComplementaryTime FactorsBlotting WesternDNA Mutational AnalysisBiologyTransfectionStatistics NonparametricImmunoenzyme TechniquesMiceOpen Reading FramesCiliogenesisGene expressionmedicineAnimalsHumansAmino Acid SequenceRNA MessengerCloning MolecularLungDNA PrimersFetusMessenger RNALungReverse Transcriptase Polymerase Chain ReactionEmbryogenesisAlternative splicingNuclear ProteinsCell DifferentiationMolecular biologyEpitheliumDNA-Binding Proteinsmedicine.anatomical_structureBronchial epithelium Asthma DevelopmentTranscription FactorsEuropean Respiratory Journal
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Rho protein inactivation induced apoptosis of cultured human endothelial cells.

2002

Small GTP-binding Rho GTPases regulate important signaling pathways in endothelial cells, but little is known about their role in endothelial cell apoptosis. Clostridial cytotoxins specifically inactivate GTPases by glucosylation [ Clostridium difficile toxin B-10463 (TcdB-10463), C. difficile toxin B-1470 (TcdB-1470)] or ADP ribosylation ( C. botulinum C3 toxin). Exposure of human umbilical cord vein endothelial cells (HUVEC) to TcdB-10463, which inhibits RhoA/Rac1/Cdc42, or to C3 toxin, which inhibits RhoA, -B, -C, resulted in apoptosis, whereas inactivation of Rac1/Cdc42 with TcdB-1470 was without effect, suggesting that Rho inhibition was responsible for endothelial apoptosis. Disruptio…

Pulmonary and Respiratory Medicinerac1 GTP-Binding Proteinrho GTP-Binding ProteinsProgrammed cell deathUmbilical VeinsEndotheliumPhysiologyBacterial ToxinsCASP8 and FADD-Like Apoptosis Regulating ProteinApoptosisBcl-2-associated X proteinBacterial ProteinsPhysiology (medical)Proto-Oncogene ProteinsmedicineCyclic AMPIn Situ Nick-End LabelingHumanscdc42 GTP-Binding ProteinCells Culturedbcl-2-Associated X ProteinAdenosine Diphosphate RibosebiologyCaspase 3Intracellular Signaling Peptides and ProteinsCell BiologyCaspase 9Cell biologyNeoplasm ProteinsEndothelial stem cellmedicine.anatomical_structureCdc42 GTP-Binding ProteinProto-Oncogene Proteins c-bcl-2Cell cultureApoptosisCaspasesbiology.proteinMyeloid Cell Leukemia Sequence 1 ProteinEndothelium VascularSignal transductionCarrier ProteinsrhoA GTP-Binding ProteinBH3 Interacting Domain Death Agonist ProteinSignal TransductionAmerican journal of physiology. Lung cellular and molecular physiology
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Amyloid-Beta Induces Different Expression Pattern of Tissue Transglutaminase and Its Isoforms on Olfactory Ensheathing Cells: Modulatory Effect of In…

2021

Abstract Alzhèimer Disease (AD) is characterized by protein aggregates in the brain, including amyloid-beta (Aβ), a substrate for tissue transglutaminase (TG2). We assessed the effect of full native peptide of Aβ (1–42), the fragments (25–35 and 35–25) on TG2 expression and its isoforms (Long and Short) on mouse Olfactory Ensheathing Cells (OECs). The levels of cytoskeletal proteins, Vimentin and Glial Fibrillary Acid Protein, were also studied. The effect of the pre-treatment with Indicaxanthin on cell viability, total Reactive Oxygen Species, superoxide anion and apoptotic pathway activation was assessed. Since Nestin is co-expressed in pluripotent stem cells with cyclin D1, their levels …

Pyridinestissue transglutaminase; olfactory ensheathing cells; amyloid-beta; oxidative stress; Indicaxanthin; self-renewalApoptosisAmyloid‐betaIndicaxanthinVimentinself-renewallcsh:ChemistryNestinMicechemistry.chemical_compoundProtein IsoformsCyclin D1lcsh:QH301-705.5SpectroscopybiologySuperoxideOpuntiaCell DifferentiationGeneral MedicineOlfactory Bulbamyloid-betaBetaxanthinsComputer Science ApplicationsCell biologyIndicaxanthinAmyloid betaTissue transglutaminase; Olfactory Ensheathing Cells; Amyloid-Beta; oxidative stress; In-dicaxanthin; self-renewalArticleGene Expression Regulation EnzymologicCatalysisInorganic ChemistryCyclin D1Alzheimer DiseaseGTP-Binding ProteinsGlial Fibrillary Acidic ProteinAnimalsHumansVimentinProtein Glutamine gamma Glutamyltransferase 2Viability assayPhysical and Theoretical ChemistryMolecular BiologyAmyloid beta-PeptidesTransglutaminasesOrganic ChemistryTissue transglutaminaseNestinSelf‐renewalNerve Regenerationlcsh:Biology (General)lcsh:QD1-999chemistryOxidative stressOlfactory ensheathing cellsbiology.proteinOlfactory ensheathing gliaReactive Oxygen SpeciesInternational Journal of Molecular Sciences
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Expression profiling of glial genes during Drosophila embryogenesis

2006

AbstractIn the central nervous system of Drosophila, the induction of the glial cell fate is dependent on the transcription factor glial cells missing (gcm). Though a considerable number of other genes have been shown to be expressed in all or in subsets of glial cells, the course of glial cell differentiation and subtype specification is only poorly understood. This prompted us to design a whole genome microarray approach comparing gcm gain-of-function and, for the first time, gcm loss-of-function genetics to wildtype in time course experiments along embryogenesis. The microarray data were analyzed with special emphasis on the temporal profile of differential regulation. A comparison of bo…

Quality ControlCell typeMicroarraysGenes InsectCell fate determinationBiologygcmGlial developmentAnimalsDrosophila ProteinsGeneMolecular BiologyOligonucleotide Array Sequence AnalysisGeneticsDrosophila embryogenesisMicroarray analysis techniquesGene Expression ProfilingDrosophila embryogenesisGene Expression Regulation DevelopmentalCell BiologyCell biologyGene expression profilingDNA-Binding ProteinsGlial cell differentiationDrosophilaDNA microarrayNeurogliaGlial genesTranscription FactorsDevelopmental BiologyDevelopmental Biology
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The Enterotoxin from Clostridium difficile (ToxA) Monoglucosylates the Rho Proteins

1995

The enterotoxin from Clostridium difficile (ToxA) is one of the causative agents of the antibiotic-associated pseudomembranous colitis. In cultured monolayer cells ToxA exhibits cytotoxic activity to induce disassembly of the actin cytoskeleton, which is accompanied by morphological changes. ToxA-induced depolymerization of actin filaments is correlated with a decrease in the ADP-ribosylation of the low molecular mass GTP-binding Rho proteins (Just, I., Selzer, J., von Eichel-Streiber, C., and Aktories, K. (1995) J. Clin. Invest. 95, 1026-1031). Here we report on the identification of the ToxA-induced modification of Rho. Applying electrospray mass spectrometry, the mass of the modification…

RHOAGlycoside HydrolasesBacterial ToxinsClostridium difficile toxin ARAC1macromolecular substancesEnterotoxinBiochemistrySubstrate SpecificityEnterotoxinsGTP-Binding ProteinsTumor Cells CulturedAmino AcidsMolecular BiologyActinbiologyMolecular massClostridioides difficileCell BiologyPseudomembranous colitisActin cytoskeletonMolecular biologycarbohydrates (lipids)GlucoseBiochemistrybiology.proteinrhoA GTP-Binding ProteinJournal of Biological Chemistry
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Rho prevents apoptosis through Bcl-2 expression: Implications for interleukin-2 receptor signal transduction

1997

Here we describe a Rho-mediated apoptosis suppression pathway driven by Bcl-2 expression in the interleukin (IL)-4- or IL-2-dependent murine T cell line TS1 alpha beta. IL-2, but not IL-4, induces Bcl-2 expression through RhoA activation which is inhibited by the specific Rho family inhibitor, Clostridium difficile Toxin B, as well as by a dominant negative RhoA mutant. Using transient transfections of RhoA mutants tagged with the vesicular stomatitis virus glycoprotein, we show that a constitutively active RhoA mutant induces Bcl-2 expression and prevents apoptosis upon IL-4 withdrawal. Finally, we have identified the signaling pathway involved together with RhoA in Bcl-2 induction and sho…

RHOAImmunologyDown-RegulationClostridium difficile toxin AApoptosisClostridium difficile toxin BTransfectionCell LineMicePhosphatidylinositol 3-Kinaseschemistry.chemical_compoundGTP-Binding ProteinsAnimalsHumansImmunology and AllergyPhosphatidylinositolProtein kinase AProtein Kinase CbiologyKinaseInterleukinReceptors Interleukin-2Molecular biologyCell biologyProto-Oncogene Proteins c-bcl-2chemistrybiology.proteinInterleukin-2Signal transductionrhoA GTP-Binding ProteinSignal TransductionEuropean Journal of Immunology
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