Search results for "Transmembrane Proteins"

showing 9 items of 9 documents

Structural Mechanism of N-Methyl-D-Aspartate Receptor Type 1 Partial Agonism

2012

N-methyl-D-aspartate (NMDA) receptors belong to a family of ionotropic glutamate receptors that contribute to the signal transmission in the central nervous system. NMDA receptors are heterotetramers that usually consist of two GluN1 and GluN2 monomers. The extracellular ligand-binding domain (LBD) of a monomer is comprised of discontinuous segments that form the functional domains D1 and D2. While the binding of a full agonist glycine to LBD of GluN1 is linked to cleft closure and subsequent ion-channel opening, partial agonists are known to activate the receptor only sub-maximally. Although the crystal structures of the LBD of related GluA2 receptor explain the mechanism for the partial a…

AgonistProtein Structuremedicine.drug_classGlycineMolecular ConformationBiophysicslcsh:MedicineMolecular Dynamics SimulationLigandsta3111Receptors N-Methyl-D-AspartateBiochemistryBiophysics Simulationsta3112Partial agonistIon ChannelsChemical BiologyMacromolecular Structure AnalysismedicineBiomacromolecule-Ligand Interactionslcsh:ScienceReceptorBiologyta116Ion channelCrystallographyMultidisciplinaryChemistrylcsh:Rta1182Glutamate receptorProteinsComputational BiologyNeurotransmittersProtein Structure TertiaryTransmembrane ProteinsBiochemistryCycloserineBiophysicsNMDA receptorLigand-gated ion channellcsh:Qhormones hormone substitutes and hormone antagonistsProtein BindingResearch ArticleNeuroscienceIonotropic effectPLoS ONE
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Oro-gustatory perception of dietary lipids and calcium signaling in taste bud cells are altered in nutritionally obesity-prone Psammomys obesus.

2013

Since the increasing prevalence of obesity is one of the major health problems of the modern era, understanding the mechanisms of oro-gustatory detection of dietary fat is critical for the prevention and treatment of obesity. We have conducted the present study on Psammomys obesus, the rodent desert gerbil which is a unique polygenic natural animal model of obesity. Our results show that obese animals exhibit a strong preference for lipid solutions in a two-bottle test. Interestingly, the expression of CD36, a lipido-receptor, in taste buds cells (TBC), isolated from circumvallate papillae, was decreased at mRNA level, but remained unaltered at protein level, in obese animals. We further st…

CD36 AntigensMaleTasteAnatomy and PhysiologyCD36BiochemistryCalcium in biologyFatschemistry.chemical_compoundMolecular Cell BiologySignaling in Cellular ProcessesMembrane Receptor Signalingchemistry.chemical_classificationMultidisciplinarybiologyQRTaste PerceptionTaste BudsLipidsSensory SystemsLipid SignalingCytochemistryThapsigarginMedicinePsammomysDisease SusceptibilityIntracellularResearch ArticleSignal Transductionmedicine.medical_specialtyThapsigarginClinical Research DesignLinoleic acidScienceLinoleic AcidFood PreferencesInternal medicinemedicineAnimalsCalcium SignalingObesityAnimal Models of DiseaseBiologyNutritionCell MembraneFatty acidProteinsbiology.organism_classificationLipid MetabolismDietary FatsGustatory SystemTransmembrane ProteinsEndocrinologyMetabolismchemistryGene Expression Regulationbiology.proteinGerbillinaeMembrane CompositionNeurosciencePLoS ONE
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Gray Matter NG2 Cells Display Multiple Ca2+-Signaling Pathways and Highly Motile Processes

2011

NG2 cells, the fourth type of glia in the mammalian CNS, receive synaptic input from neurons. The function of this innervation is unknown yet. Postsynaptic changes in intracellular Ca(2+)-concentration ([Ca(2+)](i)) might be a possible consequence. We employed transgenic mice with fluorescently labeled NG2 cells to address this issue. To identify Ca(2+)-signaling pathways we combined patch-clamp recordings, Ca(2+)-imaging, mRNA-transcript analysis and focal pressure-application of various substances to identified NG2-cells in acute hippocampal slices. We show that activation of voltage-gated Ca(2+)-channels, Ca(2+)-permeable AMPA-receptors, and group I metabotropic glutamate-receptors provo…

Central Nervous SystemAnatomy and PhysiologyVesicular glutamate transporter 1Glycobiologylcsh:MedicineHippocampal formationBiochemistryIon ChannelsTransmembrane Transport ProteinsMice0302 clinical medicinePostsynaptic potentialBiomacromolecule-Ligand Interactionslcsh:ScienceCells CulturedMembrane potential0303 health sciencesMultidisciplinarybiologyReverse Transcriptase Polymerase Chain ReactionDepolarizationNeurochemistryNeurotransmittersCell biologyElectrophysiologymedicine.anatomical_structureNeurologyNeurogliaMedicineProteoglycansNeurochemicalsGlutamateNeurogliaResearch ArticleNervous System PhysiologySignal TransductionCell PhysiologyMotilityNeuroimagingMice TransgenicNeurological System03 medical and health sciencesNeuropharmacologymedicineAnimalsHumansddc:610Biology030304 developmental biologyEndoplasmic reticulumlcsh:RProteinsGamma-Aminobutyric AcidTransmembrane ProteinsLuminescent ProteinsMicroscopy Electronnervous systemMicroscopy FluorescenceSynapsesVesicular Glutamate Transport Protein 1biology.proteinNervous System Componentslcsh:QCalciumPhysiological Processes030217 neurology & neurosurgeryNeurosciencePLoS ONE
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Role of Human Sec63 in Modulating the Steady-State Levels of Multi-Spanning Membrane Proteins

2012

The Sec61 translocon of the endoplasmic reticulum (ER) membrane forms an aqueous pore, allowing polypeptides to be transferred across or integrated into membranes. Protein translocation into the ER can occur co- and posttranslationally. In yeast, posttranslational translocation involves the heptameric translocase complex including its Sec62p and Sec63p subunits. The mammalian ER membrane contains orthologs of yeast Sec62p and Sec63p, but their function is poorly understood. Here, we analyzed the effects of excess and deficit Sec63 on various ER cargoes using human cell culture systems. The overexpression of Sec63 reduces the steady-state levels of viral and cellular multi-spanning membrane …

Gastroenterology and hepatologylcsh:MedicineProtein SynthesisEndoplasmic ReticulumBiochemistryHepatitisViral Envelope ProteinsMolecular Cell BiologyTranslocaseRNA Small Interferinglcsh:ScienceIntegral membrane proteinEndoplasmic Reticulum Chaperone BiPHeat-Shock ProteinsMultidisciplinarybiologyMembrane transport proteinReverse Transcriptase Polymerase Chain ReactionRNA-Binding ProteinsHepatitis BCellular StructuresCell biologyInfectious hepatitisCytochemistryMedicineInfectious diseasesResearch ArticleBlotting WesternViral diseasesReal-Time Polymerase Chain ReactionTransfectionCell LineSEC63Bacterial ProteinsHumansBiologyLiver diseasesDNA PrimersEndoplasmic reticulumlcsh:RCell MembraneMembrane ProteinsMembrane Transport ProteinsProteinsSEC61 TransloconChaperone ProteinsTransmembrane ProteinsLuminescent ProteinsMembrane proteinGene Expression RegulationMicroscopy FluorescenceSubcellular OrganellesChaperone (protein)Mutationbiology.proteinlcsh:QMolecular ChaperonesPLoS ONE
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Probing a Polar Cluster in the Retinal Binding Pocket of Bacteriorhodopsin by a Chemical Design Approach

2012

Bacteriorhodopsin has a polar cluster of amino acids surrounding the retinal molecule, which is responsible for light harvesting to fuel proton pumping. From our previous studies, we have shown that threonine 90 is the pivotal amino acid in this polar cluster, both functionally and structurally. In an attempt to perform a phenotype rescue, we have chemically designed a retinal analogue molecule to compensate the drastic effects of the T90A mutation in bacteriorhodopsin. This analogue substitutes the methyl group at position C(13) of the retinal hydrocarbon chain by and ethyl group (20-methyl retinal). We have analyzed the effect of reconstituting the wild-type and the T90A mutant apoprotein…

Halobacterium salinarumModels MolecularProtein FoldingProtein Denaturation01 natural sciencesBiotecnologiaBiochemistryBiophysics Simulationschemistry.chemical_compoundSensory RhodopsinsHalobacterium salinarum0303 health sciencesMultidisciplinarybiologyProtein StabilityQRTemperatureUltraviolet-visible spectroscopyThermal stabilityBacterial BiochemistryChemistryBiochemistryBacteriorhodopsinsRetinaldehydeMedicineProtonsResearch ArticleSteric effectsHydrogen bondingBioquímicaProtein StructureScienceRetinal bindingBiophysics010402 general chemistryMicrobiologyPhosphates03 medical and health sciencesBiology030304 developmental biologyAspartic AcidBinding SitesAdaptation OcularOrganic ChemistryOrganic SynthesisProteinsChromoproteinsRetinalBacteriorhodopsinBacteriologyBiological TransportChromophorebiology.organism_classification0104 chemical sciencesTransmembrane ProteinschemistryRetinaldehydeBiophysicsbiology.proteinMutant ProteinsPLoS ONE
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Polar/Ionizable Residues in Transmembrane Segments: Effects on Helix-Helix Packing

2012

The vast majority of membrane proteins are anchored to biological membranes through hydrophobic alpha-helices. Sequence analysis of high-resolution membrane protein structures show that ionizable amino acid residues are present in transmembrane (TM) helices, often with a functional and/or structural role. Here, using as scaffold the hydrophobic TM domain of the model membrane protein glycophorin A (GpA), we address the consequences of replacing specific residues by ionizable amino acids on TM helix insertion and packing, both in detergent micelles and in biological membranes. Our findings demonstrate that ionizable residues are stably inserted in hydrophobic environments, and tolerated in t…

Protein Foldinglcsh:MedicineBiochemistryBiotecnologiaProtein Structure SecondaryCell membraneGlycophorinsAmino Acidslcsh:ScienceMicelleschemistry.chemical_classificationMultidisciplinarybiologySodium Dodecyl SulfateLipidsTransmembrane proteinAmino acidmedicine.anatomical_structureBiochemistryCytochemistryThermodynamicsResearch ArticleProtein StructureBiophysicsCalcium-Transporting ATPasesProtein ChemistryProtein–protein interactionMembranes (Biologia)MicrosomesEscherichia colimedicineGlycophorinProtein InteractionsBiologyCell Membranelcsh:RMembrane ProteinsProteinsComputational BiologyBiological membraneIntracellular MembranesProtein Structure TertiaryTransmembrane ProteinsMembrane proteinchemistryHelixbiology.proteinBiophysicslcsh:QProtein Multimerization
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The skeleton of the staghorn coral Acropora millepora: molecular and structural characterization.

2014

15 pages; International audience; The scleractinian coral Acropora millepora is one of the most studied species from the Great Barrier Reef. This species has been used to understand evolutionary, immune and developmental processes in cnidarians. It has also been subject of several ecological studies in order to elucidate reef responses to environmental changes such as temperature rise and ocean acidification (OA). In these contexts, several nucleic acid resources were made available. When combined to a recent proteomic analysis of the coral skeletal organic matrix (SOM), they enabled the identification of several skeletal matrix proteins, making A. millepora into an emerging model for biomi…

ProteomicsBiomineralizationPhysiologyCoralCell Membraneslcsh:MedicineSpectrum Analysis RamanBiochemistryAcropora milleporaMaterials PhysicsSpectroscopy Fourier Transform Infraredcristallcsh:ScienceMicrostructurecorailAcetic AcidAminationExtracellular Matrix ProteinsMineralsMultidisciplinarybiologyEcologyMonosaccharidesMineralogyAnthozoaBiochemistryprotéineCoralsPhysical SciencesCellular Structures and OrganellesCrystallizationcalciteResearch ArticleMaterials ScienceProtein domainmatrice extracellulaireMarine BiologyBone and BonesCalcium CarbonateAnthozoamonosaccharideAnimals14. Life underwater[SDV.IB.BIO]Life Sciences [q-bio]/Bioengineering/BiomaterialsIntegrin bindingStaghorn corallcsh:RBiology and Life SciencesProteinsMembrane ProteinsCell Biology[ SDV.IB.BIO ] Life Sciences [q-bio]/Bioengineering/Biomaterialsbiology.organism_classificationTransmembrane ProteinsSolubilityEarth Scienceslcsh:QPhysiological ProcessesGelsFunction (biology)Biomineralization
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The hedgehog receptor patched is involved in cholesterol transport.

2011

International audience; BACKGROUND: Sonic hedgehog (Shh) signaling plays a crucial role in growth and patterning during embryonic development, and also in stem cell maintenance and tissue regeneration in adults. Aberrant Shh pathway activation is involved in the development of many tumors, and one of the most affected Shh signaling steps found in these tumors is the regulation of the signaling receptor Smoothened by the Shh receptor Patched. In the present work, we investigated Patched activity and the mechanism by which Patched inhibits Smoothened. METHODOLOGY/PRINCIPAL FINDINGS: Using the well-known Shh-responding cell line of mouse fibroblasts NIH 3T3, we first observed that enhancement …

ciliumlcsh:MedicineyeastBiochemistryReceptors G-Protein-CoupledTransmembrane Transport ProteinsMicechemistry.chemical_compound0302 clinical medicineMolecular Cell Biology[SDV.IDA]Life Sciences [q-bio]/Food engineeringMembrane Receptor SignalingBiomacromolecule-Ligand InteractionsSonic hedgehoglcsh:ScienceComputingMilieux_MISCELLANEOUS0303 health sciencesMultidisciplinaryMechanisms of Signal TransductionVeratrum Alkaloids[SDV.IDA] Life Sciences [q-bio]/Food engineeringdrosophilaSmoothened ReceptorLipidsHedgehog signaling pathwayCell biologySterolsSmoothened ReceptorAlimentation et Nutritionembryonic structurescilMembranes and Sorting[SDV.NEU]Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]Signal transductionvesicular traffickingSignal TransductionResearch Articleprimary ciliumPatched ReceptorsPatchedsignal-transductionanimal structuresCyclopamine[SPI.GPROC] Engineering Sciences [physics]/Chemical and Process EngineeringBiophysicsReceptors Cell Surfacepathway activationSaccharomyces cerevisiaetransduction du signalBiology03 medical and health sciencessonic hedgehoglipidAnimalsHumansFood and NutritionHedgehog Proteins[SPI.GPROC]Engineering Sciences [physics]/Chemical and Process EngineeringBiology030304 developmental biologyPatched Receptorsprotein signalsCell Membranelcsh:RProteinscholesterolBiological TransportTransmembrane Proteinssterol-sensing domainchemistry[ SDV.NEU ] Life Sciences [q-bio]/Neurons and Cognition [q-bio.NC]NIH 3T3 Cellscholesterol;lipid;cell trafficking; yeast;drosophila;cells ; pathway activation; vesicular trafficking; signal-transduction; sonic hedgehog;sterol-sensing domain; primary cilium;protein signalsbiology.proteincellslcsh:Qcell traffickingSmoothened030217 neurology & neurosurgery
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A genomic reappraisal of symbiotic function in the aphid/Buchnera symbiosis: reduced transporter sets and variable membrane organisations.

2011

International audience; Buchnera aphidicola is an obligate symbiotic bacterium that sustains the physiology of aphids by complementing their exclusive phloem sap diet. In this study, we reappraised the transport function of different Buchnera strains, from the aphids Acyrthosiphon pisum, Schizaphis graminum, Baizongia pistaciae and Cinara cedri, using the re-annotation of their transmembrane proteins coupled with an exploration of their metabolic networks. Although metabolic analyses revealed high interdependencies between the host and the bacteria, we demonstrate here that transport in Buchnera is assured by low transporter diversity, when compared to free-living bacteria, being mostly bas…

multidisciplinary scienceslcsh:MedicinePlant ScienceinterdépendanceBiochemistryTransmembrane Transport ProteinsBacterial Physiologylcsh:ScienceIntegral membrane proteinGeneticsbactérie0303 health sciencesPlant PestsMultidisciplinaryMicroscopy ConfocalbiologyMembrane transport protein030302 biochemistry & molecular biologybuchnera aphidicolamicroscopy confocalGenomicsHydrogen-Ion ConcentrationTransmembrane proteinFunctional GenomicsBiochemistrysymbiosis geneticsMetabolic PathwaysMetabolic Networks and PathwaysResearch Articlecell membrane ultrastructurescience and technologyMicrobiology03 medical and health sciencesMetabolic NetworksBuchneraAnimalsSymbiosisBiology030304 developmental biologyObligateCell Membranelcsh:RProteinsComputational BiologyMembrane Transport ProteinsBiological TransportBacteriologyPlant Pathologybiochemical phenomena metabolism and nutritionbiology.organism_classificationAcyrthosiphon pisumTransmembrane ProteinsaphidsMESH: SymbioseMetabolismMembrane proteinGenes Bacterialbiology.proteinlcsh:QBuchnerabuchnera aphidicola;aphids;microscopy confocal;symbiosis genetics;cell membrane ultrastructure;multidisciplinary sciences;science and technologyFunction (biology)[SDV.EE.IEO]Life Sciences [q-bio]/Ecology environment/SymbiosisPLoS ONE
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