2016
O-Glycosylation of a Secretory Granule Membrane Enzyme Is Essential for Its Endocytic Trafficking*
Vishwanatha KS, Bäck N, Lam TT, Mains RE, Eipper BA. O-Glycosylation of a Secretory Granule Membrane Enzyme Is Essential for Its Endocytic Trafficking*. Journal Of Biological Chemistry 2016, 291: 9835-9850. PMID: 26961877, PMCID: PMC4850319, DOI: 10.1074/jbc.m115.711838.Peer-Reviewed Original ResearchConceptsHigh molecular weight complexesPAM-1Molecular weight complexesEndocytic traffickingCytosolic domainBlue native PAGE analysisAtT-20 corticotrope tumor cellsWeight complexesCrucial post-translational modificationPost-translational modificationsO-glycosylation sitesPeptidylglycine αFurin-like convertasesNative PAGE analysisSoluble fragmentCorticotrope tumor cellsAlternative splicingEndocytic pathwayCatalytic domainEndocytic compartmentsGlycosylation sitesO-glycosylationMultivesicular bodiesMembrane enzymeEndoproteolytic cleavage
2014
CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain
Ostuni M, Guellec J, Hermand P, Durand P, Combadière C, Pincet F, Deterre P. CX3CL1, a chemokine finely tuned to adhesion: critical roles of the stalk glycosylation and the membrane domain. Biology Open 2014, 3: 1173-1182. PMID: 25395671, PMCID: PMC4265755, DOI: 10.1242/bio.20149845.Peer-Reviewed Original ResearchCytosolic domainTransmembrane domainChemokine domainMucin stalkMembrane domainsHigh glycosylationFunctional rolePatrolling behaviorFunctional adhesion assaysAdhesion assaysCritical roleGlycosylationDomainCytoskeletonPermanent aggregationStructural analysisStalkAdhesionRoleMembraneCX3CL1CellsAssaysReceptorsCalcium sensitive ring-like oligomers formed by synaptotagmin
Wang J, Bello O, Auclair SM, Wang J, Coleman J, Pincet F, Krishnakumar SS, Sindelar CV, Rothman JE. Calcium sensitive ring-like oligomers formed by synaptotagmin. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: 13966-13971. PMID: 25201968, PMCID: PMC4183308, DOI: 10.1073/pnas.1415849111.Peer-Reviewed Original ResearchConceptsSynaptic vesicle protein Synaptotagmin 1Cytosolic domainSoluble N-ethylmaleimide-sensitive factorN-ethylmaleimide-sensitive factorMembrane fusion machineryReceptor complex assemblyRing-like oligomersFusion machineryC2 domainComplex assemblySynaptotagmin-1Helical reconstructionFusion proceedsNovel mechanismStructural mechanismsLipid monolayersNeurotransmitter releaseAbsence of calciumPhysiological concentrationsRing formationPresence of calciumFree calcium ionsSynaptotagminCalcium influxCircular arrangement
2003
Active and Inactive Orientations of the Transmembrane and Cytosolic Domains of the Erythropoietin Receptor Dimer
Seubert N, Royer Y, Staerk J, Kubatzky KF, Moucadel V, Krishnakumar S, Smith SO, Constantinescu SN. Active and Inactive Orientations of the Transmembrane and Cytosolic Domains of the Erythropoietin Receptor Dimer. Molecular Cell 2003, 12: 1239-1250. PMID: 14636581, DOI: 10.1016/s1097-2765(03)00389-7.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineDimerizationDNA-Binding ProteinsEnzyme ActivationErythroid Precursor CellsErythropoietinJanus Kinase 2MiceMilk ProteinsModels, MolecularMolecular Sequence DataProtein Structure, QuaternaryProtein Structure, SecondaryProtein Structure, TertiaryProtein-Tyrosine KinasesProto-Oncogene ProteinsReceptors, ErythropoietinRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSequence AlignmentSignal TransductionSTAT3 Transcription FactorSTAT5 Transcription FactorTrans-ActivatorsTranscription FactorsTranscription, GeneticViral Envelope Proteins
2000
Molecular identification and functional characterization of Mdr1a in rat cholangiocytes
Gigliozzi A, Fraioli F, Sundaram P, Lee J, Mennone A, Alvaro D, Boyer J. Molecular identification and functional characterization of Mdr1a in rat cholangiocytes. Gastroenterology 2000, 119: 1113-1122. PMID: 11040198, DOI: 10.1053/gast.2000.18156.Peer-Reviewed Original ResearchMeSH KeywordsAcridinesAnimalsATP Binding Cassette Transporter, Subfamily BATP Binding Cassette Transporter, Subfamily B, Member 1ATP-Binding Cassette TransportersBile DuctsCell DivisionCell MembraneCytosolDrug Resistance, MultipleIn Vitro TechniquesIsoquinolinesKineticsMaleMicroscopy, ConfocalRatsRats, Sprague-DawleyReverse Transcriptase Polymerase Chain ReactionRhodamine 123RNA, MessengerTetrahydroisoquinolinesTranscription, GeneticVanadatesVerapamilConceptsCholangiocyte cell linePlasma membrane proteinsRat cholangiocyte cell lineCell linesCytosolic domainMembrane proteinsRhodamine 123Functional characterizationGene productsRNA transcriptsMolecular identificationMembrane subfractionsPair fragmentWestern blot analysisWestern analysisApical membraneFunctional assaysFunctional evidenceBlot analysisConfocal microscopyP-glycoprotein inhibitor verapamilRat cholangiocytesLipophilic xenobioticsReverse transcription-polymerase chain reactionDose-dependent manner
1997
Molecular Mechanism of Membrane Protein Integration into the Endoplasmic Reticulum
Mothes W, Heinrich S, Graf R, Nilsson I, von Heijne G, Brunner J, Rapoport T. Molecular Mechanism of Membrane Protein Integration into the Endoplasmic Reticulum. Cell 1997, 89: 523-533. PMID: 9160744, DOI: 10.1016/s0092-8674(00)80234-2.Peer-Reviewed Original ResearchConceptsTranslocation channelCytosolic domainTransmembrane sequenceMembrane proteinsMolecular mechanismsEndoplasmic reticulumHydrophobic transmembrane sequenceMembrane protein integrationHydrophilic polypeptide segmentsProtein integrationLipid environmentPolypeptide segmentsProteinReticulumLipid phaseSequenceMembraneRibosomesCytosolFoldingDomainMechanismAssemblySignificant implicationsTranslationSorting of Two Polytopic Proteins, the γ-Aminobutyric Acid and Betaine Transporters, in Polarized Epithelial Cells*
Perego C, Bulbarelli A, Longhi R, Caimi M, Villa A, Caplan M, Pietrini G. Sorting of Two Polytopic Proteins, the γ-Aminobutyric Acid and Betaine Transporters, in Polarized Epithelial Cells*. Journal Of Biological Chemistry 1997, 272: 6584-6592. PMID: 9045687, DOI: 10.1074/jbc.272.10.6584.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBiological TransportCarrier ProteinsCell CompartmentationCell LineCell MembraneCell PolarityCytosolDogsEndoplasmic ReticulumFluorescent Antibody Technique, IndirectGABA Plasma Membrane Transport ProteinsHumansMembrane ProteinsMembrane Transport ProteinsMolecular Sequence DataOrganic Anion TransportersReceptors, Nerve Growth FactorRecombinant Fusion ProteinsRecombinant ProteinsStructure-Activity RelationshipTransfectionConceptsCytosolic tailMadin-Darby canine kidney cellsCanine kidney cellsBetaine transporterEndoplasmic reticulumPolarized epithelial cellsTerminal cytosolic domainHuman nerve growth factor receptorKidney cellsPolytopic proteinsApical proteinsCytosolic domainChimeric transportersGrowth factor receptorApical localizationBasolateral distributionBasic residuesBasolateral localizationTransporter isoformsGAT-1Nerve growth factor receptorBgtBasolateral surfaceFactor receptorProtein
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