Search results for "Vesicle-associated membrane protein"

showing 8 items of 18 documents

Molecular and topological membrane folding determinants of transient receptor potential vanilloid 2 channel.

2015

Transient Receptor Potential (TRP) channels are related to adaptation to the environment and somatosensation. The transient receptor potential vanilloid (TRPV) subfamily includes six closely evolutionary related ion channels sharing the same domain organization and tetrameric arrangement in the membrane. In this study we have characterized biochemically TRPV2 channel membrane protein folding and transmembrane (TM) architecture. Deleting the first N-terminal 74 residues preceding the ankyrin repeat domain (ARD) show a key role for this region in targeting the protein to the membrane. We have demonstrated the co-translational insertion of the membrane-embedded region of the TRPV2 and its disp…

Models MolecularVesicle-associated membrane protein 8Protein FoldingTRPV5Protein ConformationBiophysicsTRPV Cation ChannelsBiochemistryTRPVTransient receptor potential channelAnimalsHumansProtein Structure QuaternaryMolecular BiologyIon channelTransmembrane channelsChemistryCell MembraneCell BiologyTransmembrane proteinRecombinant ProteinsAnkyrin RepeatProtein Structure TertiaryRatsHEK293 CellsBiochemistryBiophysicsAnkyrin repeatBiochemical and biophysical research communications
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Oligomerization of polytopic α-helical membrane proteins: causes and consequences

2012

Abstract Several polytopic α-helical membrane-integrated proteins appear to be organized in higher-ordered oligomeric complexes. While many aspects are still enigmatic, in recent years, the physiological impact of membrane protein oligomerization has been analyzed to some extent. In the present article, oligomerization of structurally well-defined membrane proteins is discussed. The available experimental information indicates the causes and physiological consequences of membrane protein oligomerization, including stabilization, cooperative functions, and control of specific activities. Based on the currently available observations, we aim to derive some general principles and discuss open …

Models MolecularVesicle-associated membrane protein 8Protein StabilityChemistryClinical BiochemistryPeripheral membrane proteinMembrane ProteinsBiochemistryProtein Structure SecondaryMembrane proteinBiochemistryα helicalBiophysicsHumansMolecular BiologyIntegral membrane proteinFunction (biology)G protein-coupled receptorbchm
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Targeting and membrane insertion into the endoplasmic reticulum membrane of Saccharomyces cerevisiae essential protein Rot1

2010

Rot1 is an essential yeast protein that has been related to cell wall biosynthesis, actin cytoskeleton dynamics and protein folding. Rot1 is an N -glycosylated protein anchored to the nuclear envelope–endoplasmic reticulum (ER) membrane by a transmembrane domain at its C-terminal end. Rot1 is translocated to the ER by a post-translational mechanism. Here, we investigate the protein domain required to target and translocate Rot1 to the ER membrane. We found that several deletions of the N-terminal region of Rot1 prevented neither membrane targeting nor the insertion of this protein. Interestingly, we obtained the same results when different truncated forms in the C-terminal transmembrane dom…

Sec61Vesicle-associated membrane protein 8Peripheral membrane proteinSTIM1General MedicineBiologymedicine.disease_causeApplied Microbiology and BiotechnologyMicrobiologyMembrane contact siteTransport proteinCell biologyProtein targetingmedicineIntegral membrane proteinFEMS Yeast Research
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Cloning and characterization of CSP37, a novel gene encoding a putative membrane protein of Candida albicans.

1997

In the course of an analysis of the functions and assembly of the cell wall of Candida albicans, we have cloned and characterized a gene, which we designated CSP37 (cell surface protein), encoding a 37-kDa polypeptide which is a membrane-associated protein. The gene was isolated by immunological screening of a DNA library constructed from mycelial cells with a polyclonal serum raised against cell walls of this morphology. Analysis of the nucleotide sequence of a corresponding genomic DNA fragment revealed a single open reading frame which encodes a predicted protein of 321 amino acids with no significant homology to others in the databases. Disruption of the CSP37 gene by the method describ…

Vesicle-associated membrane protein 8HeterozygoteRecombinant Fusion ProteinsMutantGenes FungalMolecular Sequence DataBiologyMicrobiologyRetinoblastoma-like protein 1Fungal ProteinsMiceHSPA2SNAP23Candida albicansEscherichia coliAnimalsAmino Acid SequenceCloning MolecularDNA FungalMolecular BiologyGeneHSPA9Mice Inbred BALB CBase SequenceHomozygoteMembrane ProteinsSequence Analysis DNABlotting NorthernMolecular biologyPhenotypeAKT1S1Gene DeletionResearch ArticleJournal of bacteriology
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Tissue expression of the vesicle protein pantophysin

1999

The cell-type restricted expression of cytoplasmic microvesicle membrane protein isoforms may be a consequence of the functional adaptation of these vesicles to the execution of specialized processes in cells of different specialization. To characterize the expression of the vesicle protein pantophysin, an isoform of the synaptic vesicle proteins synaptophysin and synaptoporin, we have prepared and characterized antibodies useful for the immunological detection of pantophysin in vitro and in situ. Using these reagents, we show by immunoblot analyses that pantophysin expression is not homogeneous but differs significantly between various bovine tissues. Furthermore, these differences are not…

Vesicle-associated membrane protein 8Membrane GlycoproteinsHistologySynaptobrevinMicrovesicleMembrane ProteinsSNAP25Cell BiologySynaptoporinBiologyCytoplasmic GranulesMolecular biologyPathology and Forensic MedicineCell biologyR-SNARE ProteinsVesicle-associated membrane proteinMembrane proteinOrgan SpecificitySynaptophysinbiology.proteinAnimalsProtein IsoformsCattleCarrier ProteinsFluorescent Antibody Technique IndirectCell and Tissue Research
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Insertion of a malE B-Galactosidase fusion protein into the envelope of Escherichia coli disrupts biogenesis of outer membrane proteins and processin…

1982

The synthesis of a membrane-bound MalE ,B-galactosidase hybrid protein, when induced by growth of Escherichia coli on maltose, leads to inhibition of cell division and eventually a reduced rate of mass increase. In addition, the relative rate of synthesis of outer membrane proteins, but not that of inner membrane proteins, was reduced by about 50%o. Kinetic experiments demonstrated that this reduction coincided with the period of maximum synthesis of the hybrid protein (and another maltose-inducible protein, LamB). The accumulation of this abnormal protein in the envelope therefore appeared specifically to inhibit the synthesis, the assembly of outer membrane proteins, or both, indicating t…

Vesicle-associated membrane protein 8MembranesPeripheral membrane proteinDNA RecombinantMembrane ProteinsPorinsBiologyMicrobiologyCell biologyTransport proteinKineticsEscheríchia coliBacterial ProteinsMembrane proteinEscherichia coliReceptors VirusOuter membrane efflux proteinsInner membraneProtein PrecursorsMaltoseBacterial outer membraneMolecular BiologyIntegral membrane proteinProteïnesBacterial Outer Membrane Proteins
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Membrane topology and post-translational modification of the Saccharomyces cerevisiae essential protein Rot1.

2007

ROT1 is an essential gene that has been related to cell wall biosynthesis, the actin cytoskeleton and protein folding. In order to help to understand its molecular function, we carried out a characterization of the Rot1 protein. It is primarily located at the endoplasmic reticulum-nuclear membrane facing the lumen. Rot1 migrates more slowly than expected, which might suggest post-translational modification. Our results indicate that Rot1 is a protein that is neither GPI-anchored nor O-glycosylated. In contrast, it is N-glycosylated. By a directed mutagenesis of several Asn residues, we identified that the protein is simultaneously glycosylated at N103, N107 and N139. Although the mutation o…

Vesicle-associated membrane protein 8Saccharomyces cerevisiae ProteinsMolecular Sequence DataBioengineeringmacromolecular substancesSaccharomyces cerevisiaeBiologyEndoplasmic ReticulumApplied Microbiology and BiotechnologyBiochemistryProtein structureSEC62Gene Expression Regulation FungalGeneticsAmino Acid SequenceCell MembraneMembrane ProteinsActin cytoskeletonCell biologyTransport proteinProtein Structure TertiaryTransmembrane domainProtein TransportBiochemistryMembrane topologyProtein foldingProtein Processing Post-TranslationalBiotechnologyMolecular ChaperonesYeast (Chichester, England)
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Probing protein interactions in the membrane-containing virus PRD1.

2015

PRD1 is a Gram-negative bacteria infecting complex tailless icosahedral virus with an inner membrane. This type virus of the family Tectiviridae contains at least 18 structural protein species, of which several are membrane associated. Vertices of the PRD1 virion consist of complexes recognizing the host cell, except for one special vertex through which the genome is packaged. Despite extensive knowledge of the overall structure of the PRD1 virion and several individual proteins at the atomic level, the locations and interactions of various integral membrane proteins and membrane-associated proteins still remain a mystery. Here, we demonstrated that blue native PAGE can be used to probe pro…

Viral Structural Proteins0303 health sciencesVesicle-associated membrane protein 8Macromolecular Substances030302 biochemistry & molecular biologyMutantMembrane ProteinsBiologyVirologyTransmembrane proteinProtein–protein interaction03 medical and health sciencesLytic cycleVirologyProtein Interaction MappingInner membraneTectiviridaeBacteriophage PRD1Electrophoresis Polyacrylamide GelProtein MultimerizationIntegral membrane protein030304 developmental biologyThe Journal of general virology
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