Search results for "TRANSMEMBRANE PROTEIN"

showing 10 items of 186 documents

Experiments Meet Hydrophobic Mismatch: A Re-evaluation Of The Orientation Of Model Transmembrane Peptides From Solid-State NMR

2009

The basic physical rules underlying the organization of biological membranes can be gathered under the simple, but powerful, concept of hydrophobic mismatch. For example, the mutual adjustment of the lipid and protein hydrophobic lengths can be related with the existence of lipid rafts and explain discrete secretory pathways in the Golgi apparatus. The orientation of membrane protein fragments is predicted to follow the same hydrophobic mismatch principles, as illustrated by some experiments and molecular dynamics simulations. However, this appears to be challenged by results of solid-state 2H NMR experiments on model transmembrane peptides, displaying tilt angle values unexpectedly small a…

Hydrophobic mismatchCrystallographyMolecular dynamicsMembraneSolid-state nuclear magnetic resonanceChemistryBiophysicsBiophysicsBiological membraneLipid bilayerLipid raftTransmembrane proteinBiophysical Journal
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Plant virus cell-to-cell movement is not dependent on the transmembrane disposition of its movement protein

2009

ABSTRACT The cell-to-cell transport of plant viruses depends on one or more virus-encoded movement proteins (MPs). Some MPs are integral membrane proteins that interact with the membrane of the endoplasmic reticulum, but a detailed understanding of the interaction between MPs and biological membranes has been lacking. The cell-to-cell movement of the Prunus necrotic ringspot virus (PNRSV) is facilitated by a single MP of the 30K superfamily. Here, using a myriad of biochemical and biophysical approaches, we show that the PNRSV MP contains only one hydrophobic region (HR) that interacts with the membrane interface, as opposed to being a transmembrane protein. We also show that a proline resi…

ImmunologyMolecular Sequence DataMicrobiologiaBiologyIlarvirusMicrobiologyCell membraneSequence Analysis ProteinVirologymedicineAmino Acid SequenceMovement proteinPeptide sequenceIntegral membrane proteinPhospholipidsEndoplasmic reticulumCircular DichroismCell MembraneProteïnes de membranaBiological membraneVirus InternalizationTransmembrane proteinCell biologyVirus-Cell InteractionsVirusPlant Viral Movement ProteinsMembranemedicine.anatomical_structureBiochemistryInsect ScienceMutationPrunusHydrophobic and Hydrophilic InteractionsSequence Alignment
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Negative regulators of integrin activity

2012

Integrins are heterodimeric transmembrane adhesion receptors composed of α- and β-subunits. They are ubiquitously expressed and have key roles in a number of important biological processes, such as development, maintenance of tissue homeostasis and immunological responses. The activity of integrins, which indicates their affinity towards their ligands, is tightly regulated such that signals inside the cell cruicially regulate the switching between active and inactive states. An impaired ability to activate integrins is associated with many human diseases, including bleeding disorders and immune deficiencies, whereas inappropriate integrin activation has been linked to inflammatory disorders…

IntegrinsIntegrin beta ChainsintegrinMolecular Sequence DataIntegrinCellActivationSHARPINta3111Collagen receptorMice03 medical and health sciences0302 clinical medicineImmune systemSDG 3 - Good Health and Well-beingCell AdhesionmedicineAnimalsHumansendocytosisAmino Acid SequenceTissue homeostasis030304 developmental biology0303 health sciencesbiologytalinta1182Cell BiologyTransmembrane proteinCell biologyadhesionmedicine.anatomical_structureIntegrin alpha Mbiology.protein/dk/atira/pure/sustainabledevelopmentgoals/good_health_and_well_beingIntegrin beta 6Integrin alpha Chains030217 neurology & neurosurgerySignal TransductionJ Cell Sci
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Resealing of large transmembrane pores produced by streptolysin O in nucleated cells is accompanied by NF‐κB activation and downstream events

2001

Streptolysin O (SLO), archetype of a cholesterol-binding bacterial cytolysin, forms large pores in the plasma membrane of mammalian cells. We have recently reported that when a limited number of pores are generated in a cell, they can be sealed in a Ca++-dependent process. Here, we show that resealing is followed by the release of IL-6 and IL-8 from keratinocytes and from endothelial cells, both relevant targets for SLO attack. Production of cytokines by these cells was preceded by activation of transcription factor nuclear factor kappaB, which thus emerges as a common denominator of stress responses to various pore-forming agents, including alpha-toxin of Staphylococcus aureus and compleme…

KeratinocytesCell Membrane PermeabilityTime FactorsBiologyBiochemistryCell LineAdenosine TriphosphateBacterial ProteinsNucleated cellGeneticsHumansInterleukin 8Molecular BiologyMicrobial toxinsMembrane permeabilizationDose-Response Relationship Drugintegumentary systemInterleukin-6Interleukin-8NF-kappa BTransmembrane proteinCell biologyStreptolysinsStreptolysinEndothelium VascularNf κb activationBiotechnologyThe FASEB Journal
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Pore-forming Staphylococcus aureus alpha-toxin triggers epidermal growth factor receptor-dependent proliferation.

2006

Staphylococcal alpha-toxin is an archetypal killer protein that homo-oligomerizes in target cells to create small transmembrane pores. The membrane-perforating beta-barrel motif is a conserved attack element of cytolysins of Gram-positive and Gram-negative bacteria. Following the recognition that nucleated cells can survive membrane permeabilization, a profile of abundant transcripts was obtained in transiently perforated keratinocytes. Several immediate early genes were found to be upregulated, reminiscent of the cellular response to growth factors. Cell cycle analyses revealed doubling of S + G2/M phase cells 26 h post toxin treatment. Determination of cell counts uncovered that after an …

KeratinocytesStaphylococcus aureusSrc Homology 2 Domain-Containing Transforming Protein 1ImmunologyCellBacterial ToxinsBlotting WesternFluorescent Antibody TechniqueTransfectionMicrobiologyCell LineHemolysin ProteinsDownregulation and upregulationNucleated cellVirologymedicineHumansGrowth factor receptor inhibitorEpidermal growth factor receptorStaphylococcus aureus alpha toxinAdaptor Proteins Signal TransducingCell Line TransformedCell ProliferationbiologyCytotoxinsReverse Transcriptase Polymerase Chain ReactionGene Expression ProfilingCell CycleCell cycleFlow CytometryTransmembrane proteinCell biologyErbB Receptorsmedicine.anatomical_structureShc Signaling Adaptor Proteinsbiology.proteinMitogensSignal TransductionCellular microbiology
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Thermodynamics of the Interaction between the Spike Protein of Severe Acute Respiratory Syndrome Coronavirus-2 and the Receptor of Human Angiotensin-…

2020

Since the end of 2019, the coronavirus SARS-CoV-2 has caused more than 1000000 deaths all over the world and still lacks a medical treatment despite the attention of the whole scientific community. Human angiotensin-converting enzyme 2 (ACE2) was recently recognized as the transmembrane protein that serves as the point of entry of SARS-CoV-2 into cells, thus constituting the first biomolecular event leading to COVID-19 disease. Here, by means of a state-of-the-art computational approach, we propose a rational evaluation of the molecular mechanisms behind the formation of the protein complex. Moreover, the free energy of binding between ACE2 and the active receptor binding domain of the SARS…

LetterPneumonia ViralProtein domainThermodynamicsPlasma protein bindingMolecular Dynamics SimulationPeptidyl-Dipeptidase ALigandsmedicine.disease_causeProtein-Protein Binding01 natural sciencesDockingBetacoronavirus03 medical and health sciencesProtein Domains0103 physical sciencesmedicineHumansGeneral Materials SciencePhysical and Theoretical ChemistryBinding siteReceptorPandemics030304 developmental biologyCoronaviruschemistry.chemical_classification0303 health sciencesBinding Sites010304 chemical physicsSARS-CoV-2Spike ProteinCOVID-19PlicamycinTransmembrane proteinEnzymechemistrySettore CHIM/03 - Chimica Generale E InorganicaMolecular Dynamics SimulationsSpike Glycoprotein CoronavirusAngiotensin-converting enzyme 2DiosminThermodynamicsAngiotensin-Converting Enzyme 2Coronavirus InfectionsProtein Binding
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Transmembrane form agrin-induced process formation requires lipid rafts and the activation of Fyn and MAPK.

2009

Overexpression or clustering of the transmembrane form of the extracellular matrix heparan sulfate proteoglycan agrin (TM-agrin) induces the formation of highly dynamic filopodia-like processes on axons and dendrites from central and peripheral nervous system-derived neurons. Here we show that the formation of these processes is paralleled by a partitioning of TM-agrin into lipid rafts, that lipid rafts and transmembrane-agrin colocalize on the processes, that extraction of lipid rafts with methyl-β-cyclodextrin leads to a dose-dependent reduction of process formation, that inhibition of lipid raft synthesis prevents process formation, and that the continuous presence of lipid rafts is requ…

MAPK/ERK pathwayanimal structuresMAP Kinase Signaling SystemChick EmbryoBiologyProto-Oncogene Proteins c-fynBiochemistryExtracellular matrixFYNMembrane MicrodomainsMolecular Basis of Cell and Developmental BiologyAnimalsSrc family kinasePseudopodiaPhosphorylationMolecular BiologyLipid raftCells CulturedMitogen-Activated Protein Kinase KinasesAgrinDose-Response Relationship Drugbeta-CyclodextrinsCell BiologyDendritesTransmembrane proteinAxonsCell biologyEnzyme Activationnervous systemPhosphorylationlipids (amino acids peptides and proteins)ChickensThe Journal of biological chemistry
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Nanovectorization of TRAIL with single wall carbon nanotubes enhances tumor cell killing

2015

International audience; Tumor necrosis factor-related apoptosis-inducing ligand (TRAIL or Apo2L) is a member of the tumor necrosis factor (TNF) superfamily. This type II transmembrane protein is able to bound specifically to cancer cell receptors (i.e., TRAIL-R1 (or DR4) and TRAIL-R2 (or DR5)) and to induce apoptosis without being toxic for healthy cells. Because membrane-bound TRAIL induces stronger receptor aggregation and apoptosis than soluble TRAIL, we proposed here to vectorize TRAIL using single-walled carbon nanotubes (SWCNTs) to mimic membrane TRAIL. Owing to their exceptional and revolutional properties, carbon nanotubes, especially SWCNTs, are used in a wide range of physical or,…

Materials science[SDV.BIO]Life Sciences [q-bio]/BiotechnologyStereochemistryCarbon nanotubesBioengineeringTRAIL02 engineering and technologyTNF-Related Apoptosis-Inducing Ligand03 medical and health sciencesMicroscopy Electron TransmissionCell Line TumorNeoplasms[SDV.BBM] Life Sciences [q-bio]/Biochemistry Molecular BiologyHumans[CHIM]Chemical SciencesGeneral Materials Science[SDV.BBM]Life Sciences [q-bio]/Biochemistry Molecular BiologyReceptor[ SDV.BBM ] Life Sciences [q-bio]/Biochemistry Molecular BiologyComputingMilieux_MISCELLANEOUS030304 developmental biologyReceptor Aggregation0303 health sciencesNanotubes CarbonMechanical Engineeringnanovector[ SDV.BIO ] Life Sciences [q-bio]/BiotechnologyGeneral Chemistry021001 nanoscience & nanotechnologyCondensed Matter PhysicsnanomedicineTransmembrane protein[SDV.BIO] Life Sciences [q-bio]/BiotechnologyReceptors TNF-Related Apoptosis-Inducing LigandCell cultureApoptosisCancer cellCancer researchcancer therapydeath receptorTumor necrosis factor alphaNanocarriers0210 nano-technology
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Fluidizing the Membrane by a Local Anesthetic: Phenylethanol Affects Membrane Protein Oligomerization

2010

The exact mechanism of action of anesthetics is still an open question. While some observations suggest specific anesthetic-protein interactions, nonspecific perturbation of the lipid bilayer has also been suggested. Perturbations of bilayer properties could subsequently affect the structure and function of membrane proteins. Addition of the local anesthetic phenylethanol (PEtOH) to model membranes and intact Escherichia coli cells not only affected membrane fluidity but also severely altered the defined helix-helix interaction within the membrane. This experimental observation suggests that certain anesthetics modulate membrane physical properties and thereby indirectly affect transmembran…

Membrane FluidityModels BiologicalProtein Structure SecondaryStructural BiologyEscherichia coliMembrane fluidityProtein Interaction Domains and MotifsAnesthetics LocalLipid bilayerMolecular BiologybiologyMembrane transport proteinChemistryEscherichia coli ProteinsCell MembranePeripheral membrane proteinMembrane ProteinsBiological membranePhenylethyl AlcoholTransmembrane proteinMembraneBiochemistryMembrane proteinbiology.proteinBiophysicsProtein MultimerizationProtein BindingSignal TransductionJournal of Molecular Biology
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Membrane-penetrating Domain of Streptolysin O Identified by Cysteine Scanning Mutagenesis

1996

Streptolysin O (SLO), a polypeptide of 571 amino acids, belongs to a family of highly homologous toxins that bind to cell membranes containing cholesterol and then polymerize to form large transmembrane pores. A conserved region close to the C terminus contains the single cysteine residue of SLO and has been implicated in membrane binding, which has been the only clear assignment of function to a part of the sequence. We have used a cysteine-less active mutant of SLO to introduce single cysteine residues at 19 positions distributed throughout the sequence. The cysteines were derivatized with the polarity-sensitive fluorophore acrylodan, and the fluorescence emission of the label was examine…

Membrane lipidsDetergentsBiochemistryCell membraneBiopolymersBacterial Proteins2-NaphthylaminemedicineCysteineCloning MolecularLipid bilayerMolecular Biologychemistry.chemical_classificationC-terminusCell MembraneCell BiologyTransmembrane proteinAmino acidmedicine.anatomical_structureSolubilitychemistryBiochemistryMutagenesisStreptolysinsStreptolysinCysteineJournal of Biological Chemistry
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