Search results for "Membrane Transport"

showing 10 items of 215 documents

Permeabilization of the Outer Mitochondrial Membrane by Bcl-2 Proteins

2010

The proteins of the Bcl-2 family regulate the release of the apoptotic factors from mitochondria during apoptosis, a key event in physiological cell death. Although their molecular mechanisms remain unclear, the Bcl-2 proteins have been proposed to directly control the permeability of the outer mitochondrial membrane by pore formation. Indeed, they share structural features with the pore forming domains of some bacterial toxins and they can give rise to proteolipidic pores in model membranes. The complex level of regulation needed to decide the fate of the cell is achieved by an intricate interaction network between different members of the family. Current models consider multiple parallel …

Mitochondrial membrane transport proteinMembranebiologyTranslocase of the outer membraneBcl-2 familyTranslocase of the inner membranebiology.proteinMitochondrionMitochondrial carrierBacterial outer membraneCell biology
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Membrane Integration of Poliovirus 2B Viroporin

2011

Virus infections can result in a variety of cellular injuries, and these often involve the permeabilization of host membranes by viral proteins of the viroporin family. Prototypical viroporin 2B is responsible for the alterations in host cell membrane permeability that take place in enterovirus-infected cells. 2B protein can be localized at the endoplasmic reticulum (ER) and the Golgi complex, inducing membrane remodeling and the blockade of glycoprotein trafficking. These findings suggest that 2B has the potential to integrate into the ER membrane, but specific information regarding its biogenesis and mechanism of membrane insertion is lacking. Here, we report experimental results of in vi…

Models MolecularFarmacologiaVesicle-associated membrane protein 8MedicinaMolecular Sequence DataImmunologyPorinsViral Nonstructural ProteinsEndoplasmic ReticulumModels BiologicalMicrobiologyAmino acid sequencesymbols.namesakeMolecular sequence dataCricetinaeVirologyAnimalsAmino Acid SequenceIntegral membrane proteinCells CulturedSequence DeletionHost cell membranebiologyMembrane transport proteinEndoplasmic reticulumGolgi apparatusBiología y Biomedicina / BiologíaVirusVirus-Cell InteractionsCell biologyPoliovirusMembraneBiochemistryCytoplasmInsect Sciencesymbolsbiology.proteinJournal of Virology
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Membrane insertion and topology of the TRanslocating chain-Associating Membrane protein (TRAM)

2011

The translocating chain-associating membrane protein (TRAM) is a glycoprotein involved in the translocation of secreted proteins into the endoplasmic reticulum (ER) lumen and in the insertion of integral membrane proteins into the lipid bilayer. As a major step toward elucidating the structure of the functional ER translocation/insertion machinery, we have characterized the membrane integration mechanism and the transmembrane topology of TRAM using two approaches: photocross-linking and truncated C-terminal reporter tag fusions. Our data indicate that TRAM is recognized by the signal recognition particle and translocon components, and suggest a membrane topology with eight transmembrane seg…

Models MolecularProtein ConformationEndoplasmic ReticulumModels BiologicalProtein Structure SecondaryMiceMembranes (Biologia)Structural BiologyAnimalsMolecular BiologyIntegral membrane proteinSignal recognition particleMembrane GlycoproteinsbiologyMembrane transport proteinPeripheral membrane proteinProteïnes de membranaIntracellular MembranesTransloconTransmembrane proteinProtein Structure TertiaryMembrane proteinBiochemistryMembrane topologybiology.proteinBiophysics
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When two turn into one: evolution of membrane transporters from half modules

2014

Abstract The recently increasing number of atomic structures for active transporters has not only revealed strong conservation in the architecture of sequence-unrelated transporter families, but also identified a unifying element called the ‘inverted repeat topology,’ which is found in nearly all transporter folds to date. Indeed, most membrane transporters consist of two or more domains with similar structure, so-called repeats. It is tempting to speculate that transporters have evolved by duplication of one repeat followed by gene fusion and modification events. An intriguing question is, whether recent genes encoding such a ‘half-transporter’ still exist as independent folding units. Alt…

Models MolecularProtein FoldingbiologyProtein familyProtein ConformationMembrane transport proteinInverted repeatClinical BiochemistryMembrane Transport ProteinsTransporterBiochemistryEvolution MolecularProtein structureBiochemistryEvolutionary biologyGene duplicationbiology.proteinAnimalsHumansProtein foldingMolecular BiologyGeneBiological Chemistry
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Functional competition within a membrane: Lipid recognition vs. transmembrane helix oligomerization

2015

Abstract Binding of specific lipids to large, polytopic membrane proteins is well described, and it is clear that such lipids are crucial for protein stability and activity. In contrast, binding of defined lipid species to individual transmembrane helices and regulation of transmembrane helix monomer–oligomer equilibria by binding of distinct lipids is a concept, which has emerged only lately. Lipids bind to single-span membrane proteins, both in the juxta-membrane region as well as in the hydrophobic membrane core. While some interactions counteract transmembrane helix oligomerization, in other cases lipid binding appears to enhance oligomerization. As reversible oligomerization is involve…

Models MolecularSyntaxin 1AMembrane lipidsLipid BilayersBiophysicsBiologyBinding CompetitiveBiochemistryProtein Structure SecondaryMembrane LipidsLipid bindingOligomerizationIntegral membrane proteinC99Transmembrane channelsMolecular StructureMembrane transport proteinCell MembranePeripheral membrane proteinMembrane ProteinsCell Biologyp24Transmembrane proteinProtein Structure TertiaryCell biologyTransmembrane domainMembrane proteinMembrane proteinbiology.proteinlipids (amino acids peptides and proteins)Protein BindingBiochimica et Biophysica Acta (BBA) - Biomembranes
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Uptake of Acidic and Basic Sugar Derivatives in Lemna gibba G1

1989

The uptake of acidic and basic sugar derivatives in Lemna gibba L. was studied. Uronic acids applied to the experimental solution (50 millimolar) induced a small decrease of the membrane potential (10 +/- 1 millivolt galacturonic acid, and 20 +/- 4 millivolt glucuronic acid). After incubation of the plants in a 0.1 millimolar solution of these substrates, no decrease in the concentration of reducing groups in the external solution was detected. Respiration increased by 31% with 50 millimolar galacturonic acid, whereas no effect was found with the same concentration of glucuronic acid. Glucosamine caused a considerable concentration-dependent membrane depolarization. ((14)C)glucosamine uptak…

Molar concentrationChromatographybiologyPhysiologyChemistryLemna gibbaSubstrate (chemistry)Plant ScienceUronic acidCarbohydrateMembrane transportbiology.organism_classificationGlucuronic acidchemistry.chemical_compoundGlucosamineGeneticsMembranes and BioenergeticsPlant Physiology
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Lactaturia and loss of sodium-dependent lactate uptake in the colon of SLC5A8-deficient mice.

2008

SLC5A8 is a member of the sodium/glucose cotransporter family. It has been proposed that SLC5A8 might act as an apical iodide transporter in the thyroid follicular cells or as a transporter of short chain monocarboxylates. We have directly addressed the functional role of SLC5A8 in vivo by generation of SLC5A8 mutant mice. We found that SLC5A8 is responsible for the re-absorption of lactate at the apical membrane of the kidney proximal tubules and of serous salivary gland ducts. In addition, SLC5A8 mediated the uptake of lactate into colonocytes under physiological conditions. We did not find any evidence of SLC5A8 being essential for the apical iodide transport in the thyroid gland, even i…

Monocarboxylic Acid Transportersmedicine.medical_specialtyColonButyrateBiologyBiochemistryIntestinal absorptionMiceInternal medicinemedicineAnimalsIodide transportLactic AcidMolecular BiologyCation Transport ProteinsMice KnockoutThyroidSodiumTransporterCell BiologyNeoplasms ExperimentalApical membraneTransport proteinButyratesMembrane Transport Structure Function and BiogenesisEndocrinologymedicine.anatomical_structureCell Transformation NeoplasticIntestinal AbsorptionCarcinogensKidney DiseasesCotransporterThe Journal of biological chemistry
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Identification of Synaptic Integration Mode in CA3 Pyramidal Neuron Model

2019

International audience; A morphologically realistic and anisotropic model of CA3 pyramidal neuron was developed to determine the synaptic integration modes the neuron is able to perform. Linearity and nonlinearity were identified in different synaptic locations with varying active mechanisms such as the presence of ionic channels in the dendritic arbor and the types of receptors in the synapse. Quantification of synaptic integration was performed using paired-pulse stimulation protocol and subthreshold input/output (sI/O) transformation. Results show that the mode of synaptic integration is location-dependent while the linearity or nonlinearity in the integration is mainly influenced by the…

MorphologyShaftsionic channelsResistancereceptorstwo-layer networksynaptic integration modesimple CA3 pyramidal neuronSynapselinear integrationdendritic arbormedicinesynaptic locationsCA3 pyramidal neuron model[SDV.IB] Life Sciences [q-bio]/BioengineeringNeuronsbiomembrane transportcomputational powerPhysicssubthreshold input-output transformationSynaptic integrationSubthreshold conductionmorphologically realistic modelMode (statistics)Linearitypaired-pulse stimulation protocolactive channelsanisotropic modelNonlinear systemmedicine.anatomical_structurenervous systemsublinear integrationCa3 pyramidal neuronbioelectric phenomena[SDV.IB]Life Sciences [q-bio]/BioengineeringAction potentialsNeuronneurophysiologysupralinear integrationNeuroscienceNeckProtocols2019 9th International IEEE/EMBS Conference on Neural Engineering (NER)
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Coordinate overexpression of two RND efflux systems, ParXY and TtgABC , is responsible for multidrug resistance in Pseudomonas putida

2020

Resistance Nodulation cell Division (RND) efflux pumps are known to contribute to the tolerance of Pseudomonas putida to aromatic hydrocarbons, but their role in antibiotic resistance has not been fully elucidated. In this study, two types of single-step multidrug-resistant (MDR) mutants were selected in vitro from reference strain KT2440. Mutants of the first type were more resistant to fluoroquinolones and β-lactams except imipenem, and overproduced the efflux system TtgABC as a result of mutations occurring in regulator TtgR. In addition to TtgABC, mutants of the second type such as HPG-5 were found to upregulate a novel RND pump, dubbed ParXY/TtgC, which accommodates cefepim, fluoroquin…

MutantGlyoxylate cycleMicrobial Sensitivity Testsmedicine.disease_causeMicrobiologyMicrobiology03 medical and health sciencesAntibiotic resistanceBacterial ProteinsDrug Resistance Multiple BacterialmedicineGeneEcology Evolution Behavior and SystematicsComputingMilieux_MISCELLANEOUS030304 developmental biology0303 health sciencesMutationbiology030306 microbiologyPseudomonas putidaMembrane Transport ProteinsBiological TransportGene Expression Regulation Bacterialbiology.organism_classificationPseudomonas putidaAnti-Bacterial AgentsMultiple drug resistance[SDV.MP]Life Sciences [q-bio]/Microbiology and ParasitologyMutationEffluxCell Division
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Distribution of the vesicular acetylcholine transporter (VAChT) in the central and peripheral nervous systems of the rat.

1994

Expression of the acetylcholine biosynthetic enzyme choline acetyltransferase (ChAT), the vesicular acetylcholine transporter (VAChT), and the high-affinity plasma membrane choline transporter uniquely defines the cholinergic phenotype in the mammalian central (CNS) and peripheral (PNS) nervous systems. The distribution of cells expressing the messenger RNA encoding the recently cloned VAChT in the rat CNS and PNS is described here. The pattern of expression of VAChT mRNA is consistent with anatomical, pharmacological, and histochemical information on the distribution of functional cholinergic neurons in the brain and peripheral tissues of the rat. VAChT mRNA-containing cells are present in…

Nervous systemMaleVesicular Acetylcholine Transport ProteinsVesicular Transport ProteinsBiologyCellular and Molecular NeuroscienceVesicular acetylcholine transportermedicineAnimalsRNA MessengerCholinergic neuronRats WistarBrain ChemistryBasal forebrainMembrane Transport ProteinsGeneral MedicineCholine acetyltransferaseRatsCholine transportermedicine.anatomical_structurenervous systemSpinal CordCholinergicGangliaCarrier ProteinsNeuroscienceAcetylcholineBiomarkersmedicine.drugJournal of molecular neuroscience : MN
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