2023
Bacterial production of recombinant contraceptive vaccine antigen from CatSper displayed on a human papilloma virus-like particle
Nand K, Jordan T, Yuan X, Basore D, Zagorevski D, Clarke C, Werner G, Hwang J, Wang H, Chung J, McKenna A, Jarvis M, Singh G, Bystroff C. Bacterial production of recombinant contraceptive vaccine antigen from CatSper displayed on a human papilloma virus-like particle. Vaccine 2023, 41: 6791-6801. PMID: 37833124, DOI: 10.1016/j.vaccine.2023.09.044.Peer-Reviewed Original ResearchConceptsVirus-like particlesSperm hyperactivated motilityHuman papilloma virusInclusion bodiesLong-acting protectionCalcium ion channelsNon-hormonal interventionsContraceptive efficacyHyperactivated motilityPapilloma virusPrincipal pieceSperm tailContraceptive vaccineBALB/c miceHypervariable regionCatSperVaccine antigensBacterial productionVaccine candidatesIon channelsIn vitroVaccinePregnancyRecombinant vaccineExtracellular loopPain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function
Jami S, Deuis J, Klasfauseweh T, Cheng X, Kurdyukov S, Chung F, Okorokov A, Li S, Zhang J, Cristofori-Armstrong B, Israel M, Ju R, Robinson S, Zhao P, Ragnarsson L, Andersson Å, Tran P, Schendel V, McMahon K, Tran H, Chin Y, Zhu Y, Liu J, Crawford T, Purushothamvasan S, Habib A, Andersson D, Rash L, Wood J, Zhao J, Stehbens S, Mobli M, Leffler A, Jiang D, Cox J, Waxman S, Dib-Hajj S, Neely G, Durek T, Vetter I. Pain-causing stinging nettle toxins target TMEM233 to modulate NaV1.7 function. Nature Communications 2023, 14: 2442. PMID: 37117223, PMCID: PMC10147923, DOI: 10.1038/s41467-023-37963-2.Peer-Reviewed Original ResearchConceptsSensory neuronsVoltage-sensing domainNav channelsTransmembrane proteinAccessory proteinsVoltage-gated sodium channelsCritical regulatorPore domainChannel gatingExtracellular loopToxin-mediated effectsNeuronal excitabilityPeptide toxinsProteinSodium channelsPharmacological activitiesNav1.7 functionKnottin peptidesNeuronsImportant insightsToxinSubunitsRegulatorDomainExcelsa
2021
Selective G protein signaling driven by substance P–neurokinin receptor dynamics
Harris J, Faust B, Gondin A, Dämgen M, Suomivuori C, Veldhuis N, Cheng Y, Dror R, Thal D, Manglik A. Selective G protein signaling driven by substance P–neurokinin receptor dynamics. Nature Chemical Biology 2021, 18: 109-115. PMID: 34711980, PMCID: PMC8712391, DOI: 10.1038/s41589-021-00890-8.Peer-Reviewed Original ResearchConceptsCryogenic-electron microscopy structuresG protein signalingGq signalingExtracellular loopG protein-coupled receptorsReceptor extracellular loopsSubstance PIntracellular signalingActive NK1RMolecular dynamics simulationsGs proteinPeptide interactionsGs signalingCognate receptorsStructural dynamicsReceptor dynamicsNeurokinin-1 receptorNeuropeptide substance PDynamics simulationsNK1R agonistNeurokinin-1ReceptorsNeurokinin ANK1RReceptor activationCryo-EM structure of an open conformation of a gap junction hemichannel in lipid bilayer nanodiscs
Khan A, Jagielnicki M, Bennett B, Purdy M, Yeager M. Cryo-EM structure of an open conformation of a gap junction hemichannel in lipid bilayer nanodiscs. Structure 2021, 29: 1040-1047.e3. PMID: 34129834, PMCID: PMC9616683, DOI: 10.1016/j.str.2021.05.010.Peer-Reviewed Original ResearchConceptsLipid bilayer nanodiscsGap junction channelsHexameric hemichannelsExtracellular loopBilayer nanodiscsTransmembrane α-helicesCryo-EM structureGap junction hemichannelsAdjacent cell membranesIntercellular conduitsCell communicationCx hemichannelsPlasma membraneOpen conformationSecond extracellular loopJunction channelsΑ-helixConformational flexibilityCell membraneHemichannelsCx isoformsExtracellular spaceNanodiscsStructural foundationMembrane
2018
hCALCRL mutation causes autosomal recessive nonimmune hydrops fetalis with lymphatic dysplasia
Mackie DI, Al Mutairi F, Davis RB, Kechele DO, Nielsen NR, Snyder JC, Caron MG, Kliman HJ, Berg JS, Simms J, Poyner DR, Caron KM. hCALCRL mutation causes autosomal recessive nonimmune hydrops fetalis with lymphatic dysplasia. Journal Of Experimental Medicine 2018, 215: 2339-2353. PMID: 30115739, PMCID: PMC6122977, DOI: 10.1084/jem.20180528.Peer-Reviewed Original ResearchConceptsStructure-function insightsG protein-coupled receptorsNovel candidate genesFirst extracellular loopProtein-coupled receptorsReceptor activity modifying proteinMutant resultsPlasma membraneCandidate genesGenetic mouse modelsExtracellular loopFrame deletionBiochemical assaysGenetic ablationReceptor chaperoneLymphatic endothelialModifying proteinsCalcitonin receptor-like receptorHuman physiologyEmbryonic demiseChaperonesMouse modelLymphatic dysplasiaReceptorsGenes
2017
Novel ecto-tagged integrins reveal their trafficking in live cells
Huet-Calderwood C, Rivera-Molina F, Iwamoto DV, Kromann EB, Toomre D, Calderwood DA. Novel ecto-tagged integrins reveal their trafficking in live cells. Nature Communications 2017, 8: 570. PMID: 28924207, PMCID: PMC5603536, DOI: 10.1038/s41467-017-00646-w.Peer-Reviewed Original ResearchConceptsIntegrin functionΒ1 integrinLive cellsCell surface adhesion receptorsHeterodimeric cell-surface adhesion receptorsIntegrin endocytosisMulticellular organismsNovel powerful toolFocal adhesionsKnockout fibroblastsIntegrin activationAdhesion receptorsExtracellular loopIntegrinsTraffickingMajor mysteriesCellsTagsAdhesionHaloTagEndocytosisPowerful toolExocytosisOrganismsVesicles
2016
N-glycosylation critically regulates function of oxalate transporter SLC26A6
Thomson RB, Thomson CL, Aronson PS. N-glycosylation critically regulates function of oxalate transporter SLC26A6. American Journal Of Physiology - Cell Physiology 2016, 311: c866-c873. PMID: 27681177, PMCID: PMC5206297, DOI: 10.1152/ajpcell.00171.2016.Peer-Reviewed Original ResearchConceptsPlasma membraneIntegral membrane proteinsCell surface deliverySLC26A6 functionTissue-specific differencesGlycosylation mutantsMembrane proteinsN-glycosylationSurface deliveryBiotinylation studiesOxalate transporterOxalate homeostasisSecond extracellular loopExtracellular loopIntact cellsEnzymatic deglycosylation studiesTransport activityEnzymatic deglycosylationFunctional studiesDeglycosylation studiesGlycosylationPutative second extracellular loopTransport functionFunctional significanceEssential role
2015
Functional Significance of Glycosylation of Cl‐/oxalate exchanger Slc26a6
Thomson R, Thomson C, Aronson P. Functional Significance of Glycosylation of Cl‐/oxalate exchanger Slc26a6. The FASEB Journal 2015, 29 DOI: 10.1096/fasebj.29.1_supplement.970.6.Peer-Reviewed Original ResearchIntrinsic transport functionTransport functionFunctional significanceSite-specific mutagenesisProtein traffickingCell surface expressionSurface deliveryBiotinylation studiesGlycosylation sitesEndocytic retrievalSecond extracellular loopExtracellular loopCell surfaceGlycosylationPutative second extracellular loopGlycan residuesTraffickingHuman SLC26A6Trafficking studiesDistinct sitesEnzyme digestionEnzymatic digestsDependent uptakeSlc26a6Glycosidic linkages
2014
N-Glycosylation Determines the Abundance of the Transient Receptor Potential Channel TRPP2*
Hofherr A, Wagner C, Fedeles S, Somlo S, Köttgen M. N-Glycosylation Determines the Abundance of the Transient Receptor Potential Channel TRPP2*. Journal Of Biological Chemistry 2014, 289: 14854-14867. PMID: 24719335, PMCID: PMC4031537, DOI: 10.1074/jbc.m114.562264.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAsparagineBinding SitesBlotting, WesternCell LineCells, CulturedGlucosidasesGlycosylationHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsLysosomesMass SpectrometryMiceMice, KnockoutMicroscopy, FluorescenceMutationPolycystic Kidney, Autosomal DominantProtein Serine-Threonine KinasesProteolysisPyruvate Dehydrogenase Acetyl-Transferring KinaseConceptsGlucosidase IINon-catalytic β-subunitsProtein expressionFirst extracellular loopAutosomal dominant polycystic liver diseaseEfficient biogenesisGenetic interactionsMembrane proteinsBiochemical approachesN-glycosylationGenetic approachesTRPP2Glycosylation sitesBiological roleLysosomal degradationΒ-subunitChemical inhibitionBiogenesisExtracellular loopNonselective cation channelsIon channelsBiological importanceGlycosylationCation channelsProtein levels
2010
A Maraviroc-Resistant HIV-1 with Narrow Cross-Resistance to Other CCR5 Antagonists Depends on both N-Terminal and Extracellular Loop Domains of Drug-Bound CCR5
Tilton JC, Wilen CB, Didigu CA, Sinha R, Harrison JE, Agrawal-Gamse C, Henning EA, Bushman FD, Martin JN, Deeks SG, Doms RW. A Maraviroc-Resistant HIV-1 with Narrow Cross-Resistance to Other CCR5 Antagonists Depends on both N-Terminal and Extracellular Loop Domains of Drug-Bound CCR5. Journal Of Virology 2010, 84: 10863-10876. PMID: 20702642, PMCID: PMC2950574, DOI: 10.1128/jvi.01109-10.Peer-Reviewed Original ResearchMeSH KeywordsBase SequenceBinding SitesCCR5 Receptor AntagonistsCell LineCohort StudiesCyclohexanesDNA PrimersDrug Resistance, ViralHIV Envelope Protein gp120HIV Fusion InhibitorsHIV InfectionsHIV-1HumansIn Vitro TechniquesMaravirocModels, BiologicalMutant ProteinsMutationPeptide FragmentsProtein Structure, TertiaryReceptors, CCR5TriazolesConceptsCCR5 antagonistsLow CCR5 levelsTreatment-experienced patientsPlasma viral RNACCR5 antagonist maravirocCourse of treatmentHigh-level resistanceMVC resistanceMVC treatmentVirologic failureExtracellular loopCCR5 levelsTreatment regimensCross-resistance profilesCXCR4 useV3 loopCCR5 useHIV entryHIV-1Viral envelope proteinsCCR5V4 loopsAntagonistMaravirocPatients
2007
Four-turn α-Helical Segment Prevents Surface Expression of the Auxiliary hβ2 Subunit of BK-type Channel*
Lv C, Chen M, Gan G, Wang L, Xu T, Ding J. Four-turn α-Helical Segment Prevents Surface Expression of the Auxiliary hβ2 Subunit of BK-type Channel*. Journal Of Biological Chemistry 2007, 283: 2709-2715. PMID: 17991741, DOI: 10.1074/jbc.m704440200.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsCell LineEndoplasmic ReticulumGene ExpressionHumansLarge-Conductance Calcium-Activated Potassium ChannelsMicroscopy, FluorescenceModels, MolecularMolecular Sequence DataMutagenesis, Site-DirectedPatch-Clamp TechniquesProtein Structure, SecondaryProtein SubunitsRatsRecombinant Fusion ProteinsSequence Homology, Amino AcidConceptsBK-type channelsSurface expressionRat chromaffin cellsExtracellular loopPancreatic beta cellsTrafficking mechanismsN-terminusDRG neuronsHelical segmentsToxin sensitivityBeta cellsClamp techniqueHelp of immunofluorescenceAuxiliary beta subunitsAlpha-helical segmentsChromaffin cellsBeta2 subunitBK channelsHbeta2Retention signalChannel regulatorRegulatory mechanismsBeta subunitEndoplasmic reticulumLarge conductance
2006
The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein*
Mazurov D, Heidecker G, Derse D. The Inner Loop of Tetraspanins CD82 and CD81 Mediates Interactions with Human T Cell Lymphotrophic Virus Type 1 Gag Protein*. Journal Of Biological Chemistry 2006, 282: 3896-3903. PMID: 17166843, DOI: 10.1074/jbc.m607322200.Peer-Reviewed Original ResearchConceptsTetraspanin-enriched microdomainsC-terminusN-terminusTetraspanin superfamily proteinsSite-directed mutationsMembrane protein complexesExtracellular loopCytoplasmic N-terminusHTLV-1T cell adhesionIntegrin functionPalmitoylated cysteinesSuperfamily proteinsProtein complexesTetraspanin CD82Cytoplasmic facePlasma membraneHTLV-1 GagColocalization approachesAmino acidsCD82IntegrinTetraspaninMutationsCD81An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization
Lerner M, Lemke D, Bertram H, Schillers H, Oberleithner H, Caplan MJ, Reinhardt J. An Extracellular Loop of the Human Non-Gastric H,K-ATPase a-subunit is Involved in Apical Plasma Membrane Polarization. Cellular Physiology And Biochemistry 2006, 18: 75-84. PMID: 16914892, DOI: 10.1159/000095169.Peer-Reviewed Original ResearchConceptsP-type ATPasesSorting motifApical deliveryExtracellular loopK-ATPaseSpecific sorting signalsPlasma membrane polarizationShort extracellular loopApical plasma membraneMadin-Darby canine kidney cellsSingle point mutationCanine kidney cellsSorting signalsGene familyPlasma membraneFlanking regionsEpithelial apical membraneK-ATPasesPhysiological roleApical membraneCellular distributionPoint mutationsIon pumpsATP1AL1Corresponding region
1999
Molecular cloning and functional characterization of KCC3, a new K-Cl cotransporter
Race J, Makhlouf F, Logue P, Wilson F, Dunham P, Holtzman E. Molecular cloning and functional characterization of KCC3, a new K-Cl cotransporter. American Journal Of Physiology 1999, 277: c1210-c1219. PMID: 10600773, DOI: 10.1152/ajpcell.1999.277.6.c1210.Peer-Reviewed Original ResearchMeSH KeywordsBiological TransportCarrier ProteinsCell LineChlorineChromosome MappingCloning, MolecularDNA PrimersEthylmaleimideGene ExpressionHumansKidneyMolecular Sequence DataOsmosisPhylogenyPlacentaPotassiumProtein Structure, TertiarySequence Homology, Amino AcidSulfhydryl ReagentsSymportersTransfectionConceptsCation-chloride cotransporter familyK-Cl cotransporterNa-Cl cotransporterTransmembrane domain 5Large extracellular loopStimulation of cotransportAmino acid levelsHydropathy analysisDeduced proteinHuman embryonic kidneyNa-K-Cl cotransporterTransmembrane domainMolecular cloningK-Cl cotransportFunctional characterizationCotransporter familyExtracellular loopEmbryonic kidneyDomain 5Amino acidsKCC3Human placentaAcid levelsSkeletal muscleCotransporterMutations in autosomal dominant polycystic kidney disease 2 gene: Reduced expression of PKD2 protein in lymphoblastoid cells
Aguiari G, Manzati E, Penolazzi L, Micheletti F, Augello G, De Vitali E, Cappelli G, Cai Y, Reynolds D, Somlo S, Piva R, del Senno L. Mutations in autosomal dominant polycystic kidney disease 2 gene: Reduced expression of PKD2 protein in lymphoblastoid cells. American Journal Of Kidney Diseases 1999, 33: 880-885. PMID: 10213643, DOI: 10.1016/s0272-6386(99)70420-8.Peer-Reviewed Original ResearchConceptsPolycystic kidney disease 2 (PKD2) geneMembrane-spanning domainsIntegral membrane proteinsLymphoblastoid cellsFirst extracellular loopAutosomal dominant polycystic kidney diseasePKD2 proteinMembrane proteinsRestriction enzyme analysisCommon genetic diseaseLymphoblastoid cell linesProtein productsMutant allelesExtracellular loopWestern blot analysisPKD2 genePolymerase chain reactionGenetic diseasesNormal proteinAmino acidsMessenger RNA levelsNonsense mutationFrameshift mutationGenesProtein
1997
An Extracellular Loop Region of the Serotonin Transporter May Be Involved in the Translocation Mechanism †
Stephan M, Chen M, Penado K, Rudnick G. An Extracellular Loop Region of the Serotonin Transporter May Be Involved in the Translocation Mechanism †. Biochemistry 1997, 36: 1322-1328. PMID: 9063880, DOI: 10.1021/bi962150l.Peer-Reviewed Original ResearchConceptsLarge extracellular loopChimeric transportersWild typeWild type SERTExtracellular loopCocaine analog 2beta-carbomethoxy-3betaCell surface biotinylationWild-type levelsSubstrate translocationExtracellular loop regionSurface biotinylationTranslocation mechanismSerotonin transporterHomologous familyType levelsConformational changesLoop regionRestriction sitesTransportersPoor expressionSubstituted regionsSynaptic cleftDrug bindingSame specificityHigh affinityExternal Cysteine Residues in the Serotonin Transporter †
Chen J, Liu-Chen S, Rudnick G. External Cysteine Residues in the Serotonin Transporter †. Biochemistry 1997, 36: 1479-1486. PMID: 9063896, DOI: 10.1021/bi962256g.Peer-Reviewed Original ResearchConceptsTransport activityMTS reagentsCysteine residuesWild typeWild-type transporterSecond external loopTransient expression systemSurface expressionRat serotonin transporterExternal cysteine residuesHydropathy analysisMutant transportersType transporterDouble mutantExpression systemMethanethiosulfonate reagentsLigand bindingSerotonin transporterMutantsExtracellular loopHeLa cellsDisulfide bondsPartial activityTransportersSerine
1992
Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump.
Jaisser F, Canessa C, Horisberger J, Rossier B. Primary sequence and functional expression of a novel ouabain-resistant Na,K-ATPase. The beta subunit modulates potassium activation of the Na,K-pump. Journal Of Biological Chemistry 1992, 267: 16895-16903. PMID: 1380956, DOI: 10.1016/s0021-9258(18)41869-8.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceBlotting, NorthernBufo marinusCell LineCloning, MolecularFemaleGene LibraryHumansIsoenzymesMacromolecular SubstancesMolecular Sequence DataOligodeoxyribonucleotidesOligonucleotides, AntisenseOocytesOuabainPotassiumRecombinant ProteinsRNASequence Homology, Nucleic AcidSodium-Potassium-Exchanging ATPaseTranscription, GeneticUrinary BladderXenopus laevisConceptsOuabain-resistant phenotypeAlpha 1 isoformBeta subunitAmino acidsK-ATPase alphaBeta 1Alpha 1Alpha 1 beta 1Oocyte expression systemXenopus laevis oocyte expression systemSequence comparisonBladder cell linesK pumpTerminal borderC-terminusExtracellular potassium ionsPrimary sequenceExpression systemMolecular mechanismsOuabain resistanceBeta 3 isoformsOuabain-resistant NaExtracellular loopFunctional expressionSubunits
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