Search results for "Membrane Biology"

showing 10 items of 12 documents

Organization into Higher Ordered Ring Structures Counteracts Membrane Binding of IM30, a Protein Associated with Inner Membranes in Chloroplasts and …

2016

The IM30 (inner membrane-associated protein of 30 kDa), also known as the Vipp1 (vesicle-inducing protein in plastids 1), has a crucial role in thylakoid membrane biogenesis and maintenance. Recent results suggest that the protein binds peripherally to membranes containing negatively charged lipids. However, although IM30 monomers interact and assemble into large oligomeric ring complexes with different numbers of monomers, it is still an open question whether ring formation is crucial for membrane interaction. Here we show that binding of IM30 rings to negatively charged phosphatidylglycerol membrane surfaces results in a higher ordered membrane state, both in the head group and in the inn…

0301 basic medicineChloroplastsMembrane lipids02 engineering and technologyBiologyBiochemistryThylakoids03 medical and health scienceschemistry.chemical_compoundMembrane LipidsBacterial ProteinsMembrane BiologyLipid bilayerProtein Structure QuaternaryMolecular BiologyPhosphatidylglycerolSynechocystisMembrane ProteinsBiological membranePhosphatidylglycerolsCell BiologySurface Plasmon Resonance021001 nanoscience & nanotechnologyKinetics030104 developmental biologyMembranechemistryBiochemistryMembrane proteinThylakoidMembrane biogenesisBiophysicsMutant ProteinsProtein Multimerization0210 nano-technologyProtein BindingThe Journal of biological chemistry
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The C-terminal Domains of Apoptotic BH3-only Proteins Mediate Their Insertion into Distinct Biological Membranes

2016

Changes in the equilibrium of pro- and anti-apoptotic members of the B-cell lymphoma-2 (Bcl-2) protein family in the mitochondrial outer membrane (MOM) induce structural changes that commit cells to apoptosis. Bcl-2 homology-3 (BH3)-only proteins participate in this process by either activating pro-apoptotic effectors or inhibiting anti-apoptotic components and by promoting MOM permeabilization. The association of BH3-only proteins with MOMs is necessary for the activation and amplification of death signals; however, the nature of this association remains controversial, as these proteins lack a canonical transmembrane sequence. Here we used an in vitro expression system to study the inserti…

0301 basic medicineProtein familyCèl·lulesBiologyBiochemistryMitochondrial Proteins03 medical and health sciencesProtein DomainsMembranes (Biologia)Protein-fragment complementation assayMembrane BiologyMicrosomesProto-Oncogene ProteinsHumansMolecular BiologyAdaptor Proteins Signal TransducingGeneticsBcl-2-Like Protein 11030102 biochemistry & molecular biologyCell MembraneBcl-2 familyProteïnes de membranaMembrane ProteinsBiological membraneCell BiologyFusion proteinTransmembrane proteinCell biology030104 developmental biologyMembraneProto-Oncogene Proteins c-bcl-2Membrane proteinB-cell lymphoma 2 (Bcl-2) family BH3-only apoptosis membrane insertion membrane protein mitochondrial apoptosis transmembrane domainApoptosis Regulatory ProteinsHydrophobic and Hydrophilic InteractionsHeLa CellsJournal of Biological Chemistry
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Alix regulates egress of hepatitis B virus naked capsid particles in an ESCRT-independent manner

2010

Hepatitis B virus (HBV) is an enveloped DNA virus that exploits the endosomal sorting complexes required for transport (ESCRT) pathway for budding. In addition to infectious particles, HBV-replicating cells release non-enveloped (nucleo)capsids, but their functional implication and pathways of release are unclear. Here, we focused on the molecular mechanisms and found that the sole expression of the HBV core protein is sufficient for capsid release. Unexpectedly, released capsids are devoid of a detectable membrane bilayer, implicating a non-vesicular exocytosis process. Unlike virions, naked capsid budding does not require the ESCRT machinery. Rather, we identified Alix, a multifunctional …

EndosomevirusesImmunologyMembrane biologyDNA virusbiochemical phenomena metabolism and nutritionGroup-specific antigenBiologyMicrobiologyVirologyExocytosisESCRTVirus ReleaseCell biologyCapsidVirologyCellular Microbiology
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Identification of Cysteine Residues in Human Cationic Amino Acid Transporter hCAT-2A That Are Targets for Inhibition by N-Ethylmaleimide

2013

In most cells, cationic amino acids such as l-arginine, l-lysine, and l-ornithine are transported by cationic (CAT) and y(+)L (y(+)LAT) amino acid transporters. In human erythrocytes, the cysteine-modifying agent N-ethylmaleimide (NEM) has been shown to inhibit system y(+) (most likely CAT-1), but not system y(+)L (Devés, R., Angelo, S., and Chávez, P. (1993) J. Physiol. 468, 753-766). We thus wondered if sensitivity to NEM distinguishes generally all CAT and y(+)LAT isoforms. Transport assays in Xenopus laevis oocytes established that indeed all human CATs (including the low affinity hCAT-2A), but neither y(+)LAT isoform, are inhibited by NEM. hCAT-2A inhibition was not due to reduced tran…

Gene isoformMutantMutation MissenseXenopusBiologyBiochemistryXenopus laevischemistry.chemical_compoundMembrane BiologyAnimalsHumansheterocyclic compoundsCysteineAmino acid transporterEnzyme InhibitorsMolecular Biologychemistry.chemical_classificationN-EthylmaleimideTransporterCell Biologybiology.organism_classificationMolecular biologyProtein Structure TertiaryAmino acidAmino Acid SubstitutionchemistryBiochemistryEthylmaleimideOocytesAmino Acid Transport Systems BasicCysteineJournal of Biological Chemistry
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A chimera carrying the functional domain of the orphan protein SLC7A14 in the backbone of SLC7A2 mediates trans-stimulated arginine transport.

2012

In human skin fibroblasts, a lysosomal transport system specific for cationic amino acids has been described and named system c. We asked if SLC7A14 (solute carrier family 7 member A14), an orphan protein assigned to the SLC7 subfamily of cationic amino acid transporters (CATs) due to sequence homology, may represent system c. Fusion proteins between SLC7A14 and enhanced GFP localized to intracellular vesicles, co-staining with the lysosomal marker LysoTracker(®). To perform transport studies, we first tried to redirect SLC7A14 to the plasma membrane (by mutating putative lysosomal targeting motifs) but without success. We then created a chimera carrying the backbone of human (h) CAT-2 and …

Lysosomal transportArginineRecombinant Fusion ProteinsProtein domainBiological Transport ActiveBiologyArginineBiochemistryCell LineXenopus laevisMembrane BiologyAnimalsHumansMolecular BiologySkinchemistry.chemical_classificationArginine transportCell BiologyMembrane transportFibroblastsHydrogen-Ion ConcentrationFusion proteinSolute carrier familyAmino acidProtein Structure TertiaryBiochemistrychemistryAmino Acid Transport Systems BasicLysosomesThe Journal of biological chemistry
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Revisiting Plant Plasma Membrane Lipids in Tobacco: A Focus on Sphingolipids

2016

International audience; The lipid composition of plasma membrane (PM) and the corresponding detergent-insoluble membrane (DIM) fraction were analyzed with a specific focus on highly polar sphingolipids, so-called glycosyl inositol phosphorylceramides (GIPCs). Using tobacco (Nicotiana tabacum) 'Bright Yellow 2' cell suspension and leaves, evidence is provided that GIPCs represent up to 40 mol % of the PM lipids. Comparative analysis of DIMs with the PM showed an enrichment of 2-hydroxylated very-long-chain fatty acid-containing GIPCs and polyglycosylated GIPCs in the DIMs. Purified antibodies raised against these GIPCs were further used for immunogold-electron microscopy strategy, revealing …

Models Molecular0106 biological sciences0301 basic medicinePhysiology[SDV]Life Sciences [q-bio]Membrane lipidsNicotiana tabacumCell Culture TechniquesMembrane biologymacromolecular substancesPlant ScienceBiology01 natural sciencesGlycosphingolipidsCell membraneMembrane Lipids03 medical and health scienceschemistry.chemical_compoundMembrane MicrodomainsTobaccoGeneticsmedicine[SDV.BV]Life Sciences [q-bio]/Vegetal BiologyInositolGlycosylcardiovascular diseasesSphingolipidsMicroscopy ConfocalCell MembraneFatty Acidstechnology industry and agriculturePhytosterolsArticlesRaftbiology.organism_classificationSphingolipidPlant Leaves030104 developmental biologymedicine.anatomical_structureBiochemistrychemistry[SDE]Environmental Sciencescardiovascular systemlipids (amino acids peptides and proteins)010606 plant biology & botanyPlant Physiology
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A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass

2000

Protein DenaturationProtein FoldingMyoglobinProtein ConformationChemistryTemperatureBiophysicsMembrane biologyTrehaloseGeneral MedicineTrehaloseReduction (complexity)Spectroscopy Mossbauerchemistry.chemical_compoundBiochemistryMyoglobinAnimalsGlassHorsesLeast-Squares AnalysisEuropean Biophysics Journal
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Protein Kinase C-dependent Ubiquitination and Clathrin-mediated Endocytosis of the Cationic Amino Acid Transporter CAT-1*

2011

Cationic amino acid transporter 1 (CAT-1) is responsible for the bulk of the uptake of cationic amino acids in most mammalian cells. Activation of protein kinase C (PKC) leads to down-regulation of the cell surface CAT-1. To examine the mechanisms of PKC-induced down-regulation of CAT-1, a functional mutant of CAT-1 (CAT-1-HA-GFP) was generated in which a hemagglutinin antigen (HA) epitope tag was introduced into the second extracellular loop and GFP was attached to the carboxyl terminus. CAT-1-HA-GFP was stably expressed in porcine aorthic endothelial and human epithelial kidney (HEK) 293 cells. Using the HA antibody internalization assay we have demonstrated that PKC-dependent endocytosis…

Swinemedia_common.quotation_subjectNedd4 Ubiquitin Protein LigasesUbiquitin-Protein LigasesUbiquitin-conjugating enzymeEndocytosisBiochemistryClathrinProtein Structure SecondaryMembrane BiologyAnimalsHumansAmino acid transporterInternalizationMolecular BiologyProtein kinase CProtein Kinase Cmedia_commonCationic Amino Acid Transporter 1biologyEndosomal Sorting Complexes Required for TransportUbiquitinationClathrin-Coated VesiclesCell BiologyReceptor-mediated endocytosisClathrinEndocytosisCell biologyUbiquitin ligaseHEK293 CellsBiochemistrybiology.protein
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Structure-function analysis of peroxisomal ATP-binding cassette transporters using chimeric dimers

2014

Background: Peroxisomal ABC transporters are predicted to function as homodimers in mammals. [br/] Results: ABCD1 interacts with ABCD2. Chimeric proteins mimicking full-length dimers represent novel tools for functional study. Artificial homodimers and heterodimers are functional. [br/] Conclusion: Interchangeability between ABCD1 and ABCD2 is confirmed, but PUFA transport depends on ABCD2. [br/] Significance: For the first time, heterodimers in mammals are proven to be functional.[br/] ABCD1 and ABCD2 are two closely related ATP-binding cassette half-transporters predicted to homodimerize and form peroxisomal importers for fatty acyl-CoAs. Available evidence has shown that ABCD1 and ABCD2 …

[SDV.BA] Life Sciences [q-bio]/Animal biologyprotéine chimereanimal diseasesATP-binding cassette transporterProximity ligation assayProtein Chimerabiochimie structurale[ SDV.BA ] Life Sciences [q-bio]/Animal biologyPolymerase Chain ReactionBiochemistryGreen fluorescent proteininteraction moléculaireMice[ CHIM.OTHE ] Chemical Sciences/Otherhomodimèrereproductive and urinary physiologyAnimal biologyhétérodimèrechemistry.chemical_classification[SDV.BA]Life Sciences [q-bio]/Animal biologymammifèreTransfectionPeroxisomeprotéine de fusionBiochemistry[CHIM.OTHE] Chemical Sciences/OtherDimerizationPlasmidsABC Transporter;Fatty Acid;Peroxisome;Protein Chimera;Protein-Protein Interactiontransporteur abcBiologyPeroxisomeCell LineProtein–protein interactionStructure-Activity RelationshipMembrane BiologyBiologie animaleparasitic diseasesAutre (Chimie)PeroxisomesAnimalsHumansMolecular BiologyDNA PrimersBase SequenceABCD2fungiABCD1Fatty acidCell BiologyFusion proteinRatsProtein-Protein InteractionABC TransporterchemistryATP-Binding Cassette TransportersOther[CHIM.OTHE]Chemical Sciences/OtherFatty Acid
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How to Bridge the Gap Between Membrane Biology and Polymer Science

1986

Can polymer chemists contribute to the understanding or even mimicking of cell membrane functions and cell-cell interactions? Fascinated by the specificity and efficiency of, for example, the destruction of tumor cells by lymphocytes (1) and having in mind what biochemical analyses tell us about membrane composition, we may try to “synthesize” membrane and cell models. The commonly used model systems, such as planar lipid monolayers at the gas-water interface, bimolecular lipid membranes and spherical liposomes, are much less stable than natural membrane systems (Figure 1).

chemistry.chemical_classificationLiposomeMaterials scienceCellMembrane biologyPolymerMembrane compositionCell membranemedicine.anatomical_structureMembranechemistryMonolayermedicineBiophysics
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