2007
Regulation of insulin secretion and GLUT4 trafficking by the calcium sensor synaptotagmin VII
Li Y, Wang P, Xu J, Gorelick F, Yamazaki H, Andrews N, Desir GV. Regulation of insulin secretion and GLUT4 trafficking by the calcium sensor synaptotagmin VII. Biochemical And Biophysical Research Communications 2007, 362: 658-664. PMID: 17720139, PMCID: PMC2194288, DOI: 10.1016/j.bbrc.2007.08.023.Peer-Reviewed Original ResearchConceptsGLUT4 trafficSyt VIIPlasma membraneGLUT4 translocationConstitutive expressionSecretory granule exocytosisSkeletal muscle cellsGLUT4 traffickingRegulated exocytosisVoltage-gated potassium channel Kv1.3Vesicular trafficSynaptotagmin VIIGLUT4 presentPotassium channel Kv1.3Calcium sensorIntracellular compartmentsDeletion resultsGlucose-stimulated insulin secretionChannel Kv1.3Granule exocytosisPancreatic beta cellsChannel activityInsulin secretionPancreatic islet cellsMuscle cells
2006
Voltage-gated potassium channel Kv1.3 regulates GLUT4 trafficking to the plasma membrane via a Ca2+-dependent mechanism
Li Y, Wang P, Xu J, Desir GV. Voltage-gated potassium channel Kv1.3 regulates GLUT4 trafficking to the plasma membrane via a Ca2+-dependent mechanism. American Journal Of Physiology - Cell Physiology 2006, 290: c345-c351. PMID: 16403947, DOI: 10.1152/ajpcell.00091.2005.Peer-Reviewed Original ResearchConceptsPlasma membraneKv1.3 channel activityAmount of GLUT4GLUT4 protein translocationInsulin sensitivityChannel activityChannel inhibitionAddition of wortmanninGLUT4 traffickingInsulin-dependent pathwayProtein translocationPeripheral insulin sensitivityVoltage-gated potassium channel Kv1.3GLUT4 translocationPotassium channel Kv1.3Gene inactivationInsulin-sensitive tissuesGLUT4 proteinKv1.3 inhibitionGlucose transportPsora-4Channel Kv1.3Adipose tissueBody weightPharmacological inhibition
1995
Primary structure and functional expression of a cGMP-gated potassium channel.
Yao X, Segal AS, Welling P, Zhang X, McNicholas CM, Engel D, Boulpaep EL, Desir GV. Primary structure and functional expression of a cGMP-gated potassium channel. Proceedings Of The National Academy Of Sciences Of The United States Of America 1995, 92: 11711-11715. PMID: 8524834, PMCID: PMC40472, DOI: 10.1073/pnas.92.25.11711.Peer-Reviewed Original ResearchMeSH KeywordsAmino Acid SequenceAnimalsBase SequenceCloning, MolecularCyclic GMPElectric ConductivityGene LibraryIon Channel GatingMolecular Sequence DataOocytesPhylogenyPotassiumPotassium ChannelsProtein BiosynthesisProtein ConformationRabbitsRNA, MessengerSequence Homology, Amino AcidTissue DistributionXenopusConceptsDeduced amino acid sequenceChannel protein phosphorylationCysteine-rich regionAmino acid sequenceNorthern blot analysisPotassium channel activityProtein phosphorylationAcid sequenceGene expressionPrimary structureFunctional expressionK channelsIon channelsChannel activityBlot analysisCyclic nucleotidesShaker K channelsPotassium channelsEffects of substancesKCN1Intracellular cGMPCGMPNitric oxideExpressionImportant role
1991
Reconstitution and partial purification of an amiloride-sensitive, cation channel from rabbit kidney
Desir G. Reconstitution and partial purification of an amiloride-sensitive, cation channel from rabbit kidney. Biochimica Et Biophysica Acta 1991, 1067: 38-42. PMID: 1868102, DOI: 10.1016/0005-2736(91)90023-2.Peer-Reviewed Original ResearchConceptsBrush border membrane vesiclesCation channelsMembrane vesicle proteinsChannel activityAmiloride-sensitive cation channelVesicle proteinsBorder membrane vesiclesMembrane vesiclesRabbit brush border membrane vesiclesProteoliposomesNative brush border membranesBrush border membraneSensitive cation channelPotassium channelsProteinPartial purificationAcridine orangeRenal brush-border membrane vesiclesBorder membraneDiethylthiadicarbocyanine iodideReconstitutionRabbit kidney