2020
Cannabinoid Type 1 Receptor is Undetectable in Rodent and Primate Cerebral Neural Stem Cells but Participates in Radial Neuronal Migration
Morozov YM, Mackie K, Rakic P. Cannabinoid Type 1 Receptor is Undetectable in Rodent and Primate Cerebral Neural Stem Cells but Participates in Radial Neuronal Migration. International Journal Of Molecular Sciences 2020, 21: 8657. PMID: 33212822, PMCID: PMC7696736, DOI: 10.3390/ijms21228657.Peer-Reviewed Original ResearchConceptsNeural stem cellsStem cellsCannabinoid type 1 receptorType 1 receptorFate determinationRadial neuronal migrationCell movementEmbryonic developmentIntracellular vesiclesCellular locationMRNA sequencingMolecular mechanismsCortical plateElectron microscopic reconstructionCellular proliferationNeuronal migrationZone cellsSubventricular zone cellsEmbryonic miceMolecular substratesSVZ cellsMicroscopic reconstructionRecreational cannabis useMacaque cerebral cortexPrimate neuronsAdaptive Regulation of Hepatocyte Transporters in Cholestasis
Boyer J. Adaptive Regulation of Hepatocyte Transporters in Cholestasis. 2020, 378-389. DOI: 10.1002/9781119436812.ch31.Peer-Reviewed Original ResearchSignal transduction pathwaysAdaptive responseOrganic solute transporterSecretory polarityTranscription factorsTransduction pathwaysMolecular adaptationsSolute transportersCytoskeleton structureIntracellular vesiclesTarget genesMembrane transportersCellular eventsJunctional proteinsNuclear receptorsCanalicular domainCholestatic phenotypeTransportersTight junctionsVital functionsRegulationAdaptive regulationImportant ligandsEnzymatic reactionsBile salt synthesis
2019
Role of a patatin-like phospholipase in Plasmodium falciparum gametogenesis and malaria transmission
Singh P, Alaganan A, More K, Lorthiois A, Thiberge S, Gorgette O, Guillotte Blisnick M, Guglielmini J, Aguilera S, Touqui L, Singh S, Chitnis C. Role of a patatin-like phospholipase in Plasmodium falciparum gametogenesis and malaria transmission. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 17498-17508. PMID: 31413195, PMCID: PMC6717283, DOI: 10.1073/pnas.1900266116.Peer-Reviewed Original ResearchConceptsFemale gametesPerforin-like proteinBlood-stage growthIngestion of gametocytesProcess of gametogenesisPatatin-like phospholipaseGamete egressDiverse organismsMembrane remodelingIntracellular vesiclesVesicle secretionVesicular dischargeMale gametesOocyst formationPeripheral membraneGametocyte developmentGametogenesisExtensive membraneConditional deletionGametesBlood mealDevelopment of drugsDeletionPotential targetGenes
2016
Optogenetic activation reveals distinct roles of PIP3 and Akt in adipocyte insulin action
Xu Y, Nan D, Fan J, Bogan JS, Toomre D. Optogenetic activation reveals distinct roles of PIP3 and Akt in adipocyte insulin action. Journal Of Cell Science 2016, 129: 2085-2095. PMID: 27076519, PMCID: PMC4878990, DOI: 10.1242/jcs.174805.Peer-Reviewed Original ResearchConceptsPI3KGLUT4 translocationDistinct rolesAkt-independent pathwayNew optogenetic toolsGlucose transporter 4Drug-mediated inhibitionTranslocation responseIntracellular vesiclesOverall insulin actionPlasma membraneInsulin actionN-terminusOptogenetic toolsInsulin stimulationTransporter 4Biochemical assaysAktTranslocationAdipose cellsVesiclesPathwayCIB1PIP3Cells
2015
Actin Depletion Initiates Events Leading to Granule Secretion at the Immunological Synapse
Ritter A, Asano Y, Stinchcombe J, Dieckmann N, Chen B, Gawden-Bone C, van Engelenburg S, Legant W, Gao L, Davidson M, Betzig E, Lippincott-Schwartz J, Griffiths G. Actin Depletion Initiates Events Leading to Granule Secretion at the Immunological Synapse. Immunity 2015, 42: 864-876. PMID: 25992860, PMCID: PMC4448150, DOI: 10.1016/j.immuni.2015.04.013.Peer-Reviewed Original ResearchConceptsCytotoxic T lymphocytesT cell receptorActin-rich projectionsCortical actin densityActin depletionCortical actinCentrosome polarizationPolarized secretionActin densityIntracellular vesiclesRegulate secretionCentrosomeImmunological synapseActinSynapse maturationGranule secretionT lymphocytesTumor cellsPhospholipid PIP2Area of membraneSynapseSecretionCSMACHigh-resolution 4D imagingInitial event
2007
MAL decreases the internalization of the aquaporin-2 water channel
Kamsteeg EJ, Duffield AS, Konings IB, Spencer J, Pagel P, Deen PM, Caplan MJ. MAL decreases the internalization of the aquaporin-2 water channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 2007, 104: 16696-16701. PMID: 17940053, PMCID: PMC2034241, DOI: 10.1073/pnas.0708023104.Peer-Reviewed Original ResearchConceptsAquaporin-2 water channelIntracellular vesiclesApical membrane proteinsMembrane-associated proteinsTrafficking of AQP2Apical surface expressionEpithelial cellsCell surface retentionApical plasma membraneInvolvement of MALBody water homeostasisS256 phosphorylationWater channel proteinsSurface expressionApical deliveryRegulated traffickingSorting eventsRenal epithelial cellsMembrane associationMembrane proteinsPosttranslational modificationsProtein interactionsPlasma membraneChannel proteinsWater channels
2005
Two CD1 genes map to the chicken MHC, indicating that CD1 genes are ancient and likely to have been present in the primordial MHC
Salomonsen J, Sørensen M, Marston D, Rogers S, Collen T, van Hateren A, Smith A, Beal R, Skjødt K, Kaufman J. Two CD1 genes map to the chicken MHC, indicating that CD1 genes are ancient and likely to have been present in the primordial MHC. Proceedings Of The National Academy Of Sciences Of The United States Of America 2005, 102: 8668-8673. PMID: 15939887, PMCID: PMC1150808, DOI: 10.1073/pnas.0409213102.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsAntigens, CD1Base SequenceBlotting, SouthernChickensChromosome MappingCloning, MolecularCluster AnalysisComputational BiologyDNA PrimersDNA, ComplementaryEvolution, MolecularFlow CytometryMajor Histocompatibility ComplexMolecular Sequence DataPhylogenySequence Analysis, DNAConceptsCD1 genesChicken MHCCD1 systemPrimordial MHCDraft chicken genome sequenceChicken genome sequenceAncestor of mammalsClassical class I genesClass I genesGenome sequenceTranscriptional orientationCD1 isotypesPhylogenetic analysisSequence analysisI geneCD1 moleculesBackcross familiesSouthern blottingIntracellular vesiclesChicken linesII genesGenesSequenceRNA expressionNKT cells
2002
Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane
Deen PM, Van Balkom BW, Savelkoul PJ, Kamsteeg EJ, Van Raak M, Jennings ML, Muth TR, Rajendran V, Caplan MJ. Aquaporin-2: COOH terminus is necessary but not sufficient for routing to the apical membrane. American Journal Of Physiology. Renal Physiology 2002, 282: f330-f340. PMID: 11788448, DOI: 10.1152/ajprenal.0168.2001.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsAquaporin 1Aquaporin 2Aquaporin 6AquaporinsArginine VasopressinBlood Group AntigensCell CompartmentationCell FractionationCell LineCell MembraneCell Membrane PermeabilityColforsinEndocytosisGene ExpressionHumansKidneyProtein Structure, TertiaryProtein TransportRatsRecombinant Fusion ProteinsVasoconstrictor AgentsWaterConceptsIntracellular vesiclesApical membraneAquaporin-2Wild‐type aquaporin‐2Mammalian water homeostasisMadin-Darby canine kidney cellsCanine kidney cellsAQP2 accumulationPrimary sequenceSame proteinOsmotic water permeabilityApical expressionForskolin treatmentAquaporin-1 (AQP1) water channelWater homeostasisKidney cellsBasolateral membraneVesiclesPlacental alkaline phosphataseMembraneWater channelsDuct cellsAQP1TailCells
2000
Prostaglandin E2 interaction with AVP: effects on AQP2 phosphorylation and distribution
Zelenina M, Christensen B, Palmér J, Nairn A, Nielsen S, Aperia A. Prostaglandin E2 interaction with AVP: effects on AQP2 phosphorylation and distribution. American Journal Of Physiology. Renal Physiology 2000, 278: f388-f394. PMID: 10710543, DOI: 10.1152/ajprenal.2000.278.3.f388.Peer-Reviewed Original ResearchConceptsTranslocation of AQP2AQP2 phosphorylationPlasma membraneAquaporin-2Subcellular distributionPlasma membrane-enriched fractionVesicle-enriched fractionsMembrane-enriched fractionDuct water permeabilityConsensus sitesIntracellular vesiclesPhosphorylationDifferential centrifugation techniqueAction of arginineRenal inner medullaE2 interactionRat renal inner medullaTranslocationInner medullaDose-dependent mannerWater channelsMembraneDephosphorylationTraffickingProtein
1997
Ion exchangers mediating NaCl transport in the proximal tubule.
Aronson PS. Ion exchangers mediating NaCl transport in the proximal tubule. Wiener Klinische Wochenschrift 1997, 109: 435-40. PMID: 9261983.Commentaries, Editorials and LettersConceptsApical membraneBasolateral membraneBrush border membraneMembrane traffickingNHE3 protein expressionMembrane ion exchangerIntracellular vesiclesMammalian proximal tubuleBorder membraneDifferential regulationProximal tubule cellsInhibitor sensitivityPossible regulationFormate transportExchange activityProtein expressionCl- channelsTubule cellsMembranePolyclonal antibodiesVesiclesCellsNHE3Oxalate-sulfate exchangeRegulation
1994
Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells.
Matovcik LM, Karapetian O, Czernik AJ, Marino CR, Kinder BK, Gorelick FS. Antibodies to an epitope on synapsin I detect a protein associated with the endocytic compartment in non-neuronal cells. European Journal Of Cell Biology 1994, 65: 327-40. PMID: 7536673.Peer-Reviewed Original ResearchConceptsClone 9 cellsEndocytic compartmentsPotential substrate proteinsDependent protein kinase IISynapsin ISmall intracellular vesiclesProtein kinase IIRat liver endosomesSubstrate proteinsPhosphorylation sequenceNon-neuronal cellsCLIP-170Intracellular vesiclesKinase IILarge endosomesPostnuclear supernatantEndosomesSensitive compartmentLiver endosomesProteinConfocal microscopyCell linesVesiclesIntestinal enterocytesCompartments
1993
Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly
Gottardi CJ, Caplan MJ. Molecular requirements for the cell-surface expression of multisubunit ion-transporting ATPases. Identification of protein domains that participate in Na,K-ATPase and H,K-ATPase subunit assembly. Journal Of Biological Chemistry 1993, 268: 14342-14347. PMID: 8390991, DOI: 10.1016/s0021-9258(19)85246-8.Peer-Reviewed Original ResearchConceptsK-ATPase alpha subunitK-ATPase beta subunitAlpha subunitBeta subunitCell surface expressionTerminal halfK-ATPaseCell surface deliveryEfficient cell surface expressionK-ATPase alphaNH2-terminal halfCOS-1 cellsIon-transporting ATPasesProtein domainsK-ATPase enzymeSubunit assemblySurface deliveryIntracellular vesiclesSubunit chimerasIndividual subunitsActive enzymeMolecular requirementsSubunitsCell surfaceBeta protein
This site is protected by hCaptcha and its Privacy Policy and Terms of Service apply