Search results for "Membrane transport protein"

showing 10 items of 159 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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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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New methods to improve the safety assessment of cryopreserved ovarian tissue for fertility preservation in breast cancer patients

2015

Objective To develop a novel molecular panel of markers to detect breast cancer (BC) disseminated malignant cells in ovarian tissue, and to improve the safety of ovarian tissue transplantation. Design Experimental study. Setting University hospital. Patient(s) Ten ovarian biopsies from healthy patients, 13 biopsies with diagnosed BC metastasis, and 4 biopsies from primary BC tumor for designing a diagnostic panel of BC cell contamination; 60 ovarian biopsies from BC patients undergoing fertility preservation for validating the panel. Animal(s) Female nude mice. Intervention(s) A novel panel for BC malignant cell detection by reverse-transcription polymerase chain reaction (RT-PCR), inmmunoh…

OncologyPathologyBiopsyMetastasisPregnancyRisk FactorsMedicineOvarian tissue cryopreservationFertility preservationMUC1Ovarian Neoplasmsmedicine.diagnostic_testReverse Transcriptase Polymerase Chain ReactionMammaglobin AFertility PreservationObstetrics and GynecologyMiddle AgedImmunohistochemistrymedicine.anatomical_structureNeoplasm MicrometastasisHeterograftsFemaleInfertility FemaleAdultmedicine.medical_specialtyReproductive Techniques AssistedMice NudeBreast NeoplasmsOvaryBreast cancerPredictive Value of TestsInternal medicineBiopsyBiomarkers TumorAnimalsHumansNeoplasm InvasivenessAgedGlycoproteinsCryopreservationbusiness.industryOvaryMucinsMembrane Transport ProteinsReproducibility of Resultsmedicine.diseaseTransplantationFertilityReproductive MedicineCase-Control StudiesCarrier ProteinsbusinessFertility and Sterility
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The stability and functional properties of proteoliposomes mixed with dextran derivatives bearing hydrophobic anchor groups

1992

Liposomes composed of Escherichia coli phospholipid were coated with polysaccharides bearing hydrophobic palmitoyl anchors. The effect on the stability of liposomes without or with integral membrane proteins was investigated. A high concentration of hydrophobized dextrans protected the liposomes against detergent degradation, decreased the fluidity of the membranes, prevented fusion of the liposomes and enhanced their stability. Proteoliposomes containing beef heart cytochrome-c oxidase and the lactose transport carrier of E. coli were similarly affected by coating with the dextrans. Under these conditions both membrane proteins were still active. Long-term stability of the coated liposomes…

PROTEINMembrane FusionBiochemistryMembrane Potentialschemistry.chemical_compoundFUSIONINTEGRAL MEMBRANE PROTEINBINDINGIntegral membrane proteinLiposomeSymportersEscherichia coli ProteinsVesiclePROTEOLIPOSOMEDextransDEXTRAN DERIVATIVEBIOLOGICAL-MEMBRANESFluoresceinsMembraneCarbohydrate SequenceESCHERICHIA-COLIMonosaccharide Transport ProteinsCations DivalentMembrane FluidityProteolipidsMolecular Sequence DataBiophysicsPhospholipidFluorescence PolarizationLactose transportOXIDASECYTOCHROME-CVESICLESElectron Transport Complex IVHYDROPHOBIC ANCHOR GROUPEscherichia coliAnimalsKINETICSChromatographyMyocardiumMembrane ProteinsMembrane Transport ProteinsBiological membraneCell BiologyPROTON-MOTIVE FORCEMembrane proteinchemistryLiposomesCalciumCattleBiochimica et Biophysica Acta (BBA) - Biomembranes
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The Arabidopsis COPT6 Transport Protein Functions in Copper Distribution Under Copper-Deficient Conditions

2013

Copper (Cu), an essential redox active cofactor, participates in fundamental biological processes, but it becomes highly cytotoxic when present in excess. Therefore, living organisms have established suitable mechanisms to balance cellular and systemic Cu levels. An important strategy to maintain Cu homeostasis consists of regulating uptake and mobilization via the conserved family of CTR/COPT Cu transport proteins. In the model plant Arabidopsis thaliana, COPT1 protein mediates root Cu acquisition, whereas COPT5 protein functions in Cu mobilization from intracellular storage organelles. The function of these transporters becomes critical when environmental Cu bioavailability diminishes. Ho…

PhysiologyMolecular Sequence DataSaccharomyces cerevisiaeMutantArabidopsisSaccharomyces cerevisiaePlant SciencePlant RootsCofactorCell membraneGene Expression Regulation PlantArabidopsisOrganellemedicineHomeostasisAmino Acid SequenceSLC31 ProteinsbiologyArabidopsis ProteinsMembrane transport proteinCell MembraneGenetic Complementation TestMembrane Transport ProteinsBiological TransportCell BiologyGeneral MedicinePlants Genetically Modifiedbiology.organism_classificationUp-RegulationTransport proteinCell biologyPlant LeavesMutagenesis Insertionalmedicine.anatomical_structureBiochemistrySeedsbiology.proteinPlant Vascular BundleSequence AlignmentCopperPlant ShootsPlant and Cell Physiology
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