2024
Sustained caloric restriction potentiates insulin action by activating prostacyclin synthase
Merali C, Quinn C, Huffman K, Pieper C, Bogan J, Barrero C, Merali S. Sustained caloric restriction potentiates insulin action by activating prostacyclin synthase. Obesity 2024 PMID: 39420421, DOI: 10.1002/oby.24150.Peer-Reviewed Original ResearchMolecular mechanismsIncreased GLUT4 translocationComplex molecular mechanismsGlucose uptake regulationUBX domainIncreased glucose uptakeGLUT4 translocationGLUT4 functionCaloric restrictionPTGIS expressionProteomic profilingCell surfaceCleavage pathwayInsulin sensitivityHuman adipocytesAdipose tissueGlucose uptakeGLUT4Enhanced insulin sensitivityInsulin receptor densityInsulin actionRisk of metabolic disordersCell membraneProstacyclin synthaseMonths of CR
2023
The glucose transporter GLUT4 tethers RIG-I-like receptors to suppress antiviral immunity
Harrison A, Yang D, Cahoon J, Geng T, Karginov T, Torrance B, Chiari C, Haynes L, Vella A, Witczak C, Bogan J, Wang P. The glucose transporter GLUT4 tethers RIG-I-like receptors to suppress antiviral immunity. The Journal Of Immunology 2023, 210: 161.17-161.17. DOI: 10.4049/jimmunol.210.supp.161.17.Peer-Reviewed Original ResearchGlucose transporter 4Plasma membraneTranslocation of GLUT4Reversible posttranslational modificationRLR activationAntiviral immunityCytosolic immune sensorsVesicular traffickingPosttranslational modificationsCanonical roleCellular metabolismImmunometabolic regulationIntracellular compartmentsNovel linkTransporter 4Genetic ablationNovel mechanismImmune sensorsDistinct phenotypesLike receptorsCurrent dogmaReceptor regulationRLRIFN responseLike receptor regulation
2022
Ubiquitin-like processing of TUG proteins as a mechanism to regulate glucose uptake and energy metabolism in fat and muscle
Bogan JS. Ubiquitin-like processing of TUG proteins as a mechanism to regulate glucose uptake and energy metabolism in fat and muscle. Frontiers In Endocrinology 2022, 13: 1019405. PMID: 36246906, PMCID: PMC9556833, DOI: 10.3389/fendo.2022.1019405.Peer-Reviewed Original ResearchConceptsGolgi matrixTUG ProteinVesicle cargoC-terminal productInsulin stimulationN-degron pathwayGLUT4 storage vesiclesCell surfaceUbiquitin-like proteinGLUT4 glucose transportersGlucose uptakeAspects of physiologyN-terminal cleavage productMuscle cellsP97 ATPaseCleavage productsC-terminusFatty acid oxidationGene expressionSingle proteinN-terminusMatrix proteinsEndoproteolytic cleavageCell typesGlucose transporterInhibitors of RNA and protein synthesis cause Glut4 translocation and increase glucose uptake in adipocytes
Meriin AB, Zaarur N, Bogan JS, Kandror KV. Inhibitors of RNA and protein synthesis cause Glut4 translocation and increase glucose uptake in adipocytes. Scientific Reports 2022, 12: 15640. PMID: 36123369, PMCID: PMC9485115, DOI: 10.1038/s41598-022-19534-5.Peer-Reviewed Original ResearchConceptsInhibitors of RNAGLUT4 translocationProtein synthesisEndocytosis of GLUT4Glucose uptakeRecycling of transferrinGlucose transporter 4Actinomycin DBiosynthesis de novoSignaling proteinsPlasma membraneTransporter 4Intracellular retentionContinuous RNATranslocationRNADe novoAdipocytesVesiclesInhibitorsTBC1D4UptakeEndocytosisGLUT4Exocytosis
2021
Insulin-stimulated endoproteolytic TUG cleavage links energy expenditure with glucose uptake
Habtemichael EN, Li DT, Camporez JP, Westergaard XO, Sales CI, Liu X, López-Giráldez F, DeVries SG, Li H, Ruiz DM, Wang KY, Sayal BS, González Zapata S, Dann P, Brown SN, Hirabara S, Vatner DF, Goedeke L, Philbrick W, Shulman GI, Bogan JS. Insulin-stimulated endoproteolytic TUG cleavage links energy expenditure with glucose uptake. Nature Metabolism 2021, 3: 378-393. PMID: 33686286, PMCID: PMC7990718, DOI: 10.1038/s42255-021-00359-x.Peer-Reviewed Original ResearchConceptsTUG cleavageGlucose uptakeProtein degradation pathwaysGLUT4 glucose transportersCoactivator PGC-1αC-terminal cleavage productInsulin-stimulated glucose uptakeAte1 arginyltransferaseGene expressionPhysiological relevanceWhole-body energy expenditureGlucose transporterPeroxisome proliferator-activated receptorCell surfacePGC-1αProtein 1Proliferator-activated receptorDegradation pathwayEffect of insulinCleavage pathwayAdipose cellsCleavage productsPathwayCleavageEnergy expenditureGranular detail of β cell structures for insulin secretion
Bogan JS. Granular detail of β cell structures for insulin secretion. Journal Of Cell Biology 2021, 220: e202012082. PMID: 33427875, PMCID: PMC7802365, DOI: 10.1083/jcb.202012082.Commentaries, Editorials and Letters
2019
Vasopressin inactivation: Role of insulin-regulated aminopeptidase
Li DT, Habtemichael EN, Bogan JS. Vasopressin inactivation: Role of insulin-regulated aminopeptidase. Vitamins & Hormones 2019, 113: 101-128. PMID: 32138946, DOI: 10.1016/bs.vh.2019.08.017.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsInsulin-regulated aminopeptidaseInsulin-responsive glucose transporterHuman placental leucine aminopeptidaseMetabolic syndromeInsulin resistanceVasopressin secretionUBX domainCoordinated regulationGenetic variationAbsence of insulinGLUT4 proteinGestational diabetes insipidusPotential pathophysiologic rolePhysiological importanceGlucose transporterCell surfaceProteolytic cleavageNovel insightsPlacental leucine aminopeptidaseRodent homologueVasopressinase activityLeucine aminopeptidasePathophysiologic mechanismsMuscle cellsPathophysiologic roleAcylation – A New Means to Control Traffic Through the Golgi
Ernst AM, Toomre D, Bogan JS. Acylation – A New Means to Control Traffic Through the Golgi. Frontiers In Cell And Developmental Biology 2019, 7: 109. PMID: 31245373, PMCID: PMC6582194, DOI: 10.3389/fcell.2019.00109.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsDiverse protein clientsSorting of proteinsIntegral membrane proteinsProtein clientsS-acylationGolgi networkProtein adaptersMembrane proteinsAnterograde fluxLipid modificationGolgi cisternaeGolgiLipid acylationNeurodegenerative diseasesHuman physiologyProteinPotential relevanceOrganellesRecent dataRapid trafficAcylationCisternaePhysiologyCargoMechanism
2018
Usp25m protease regulates ubiquitin-like processing of TUG proteins to control GLUT4 glucose transporter translocation in adipocytes
Habtemichael EN, Li DT, Alcázar-Román A, Westergaard XO, Li M, Petersen MC, Li H, DeVries SG, Li E, Julca-Zevallos O, Wolenski JS, Bogan JS. Usp25m protease regulates ubiquitin-like processing of TUG proteins to control GLUT4 glucose transporter translocation in adipocytes. Journal Of Biological Chemistry 2018, 293: 10466-10486. PMID: 29773651, PMCID: PMC6036200, DOI: 10.1074/jbc.ra118.003021.Peer-Reviewed Original ResearchMeSH KeywordsAdipocytesAnimalsCarrier ProteinsCell MembraneCells, CulturedGlucoseGlucose Transporter Type 4Hypoglycemic AgentsInsulinIntracellular Signaling Peptides and ProteinsKinesinsMaleMiceMice, Inbred C57BLMotor ActivityProtein TransportProteolysisRatsRats, Sprague-DawleySignal TransductionUbiquitinUbiquitin ThiolesteraseConceptsGLUT4 storage vesiclesTUG cleavageGolgi matrixPlasma membraneGLUT4 glucose transporter translocationMicrotubule-based movementUbiquitin-like proteinGLUT4 glucose transportersStorage vesiclesGlucose transporter translocationAttenuation of insulinKinesin motor proteinsGLUT4 vesiclesSpecialized vesiclesGLUT4 translocationTransporter translocationSplice formsMotor proteinsProtein trapProtein abundanceProteolytic pathwayDiet-induced insulin resistanceEndoproteolytic cleavageGlucose transporterProteolytic processing
2015
Coordinated Regulation of Vasopressin Inactivation and Glucose Uptake by Action of TUG Protein in Muscle*
Habtemichael EN, Alcázar-Román A, Rubin BR, Grossi LR, Belman JP, Julca O, Löffler MG, Li H, Chi NW, Samuel VT, Bogan JS. Coordinated Regulation of Vasopressin Inactivation and Glucose Uptake by Action of TUG Protein in Muscle*. Journal Of Biological Chemistry 2015, 290: 14454-14461. PMID: 25944897, PMCID: PMC4505512, DOI: 10.1074/jbc.c115.639203.Peer-Reviewed Original ResearchConceptsInsulin-regulated aminopeptidaseVesicle translocationGLUT4 intracellular retentionGlucose uptakeT-tubule fractionTransgenic miceTransmembrane aminopeptidaseAQP2 water channelsTUG ProteinCoordinated regulationGLUT4 translocationInsulin stimulationPhysiological importanceGlucose transporterProteolytic processingIntracellular retentionTranslocationWater homeostasisMuscle cellsGLUT4Skeletal muscleShort peptidesProteolysisProteinAbundanceAcetylation of TUG Protein Promotes the Accumulation of GLUT4 Glucose Transporters in an Insulin-responsive Intracellular Compartment*
Belman JP, Bian RR, Habtemichael EN, Li DT, Jurczak MJ, Alcázar-Román A, McNally LJ, Shulman GI, Bogan JS. Acetylation of TUG Protein Promotes the Accumulation of GLUT4 Glucose Transporters in an Insulin-responsive Intracellular Compartment*. Journal Of Biological Chemistry 2015, 290: 4447-4463. PMID: 25561724, PMCID: PMC4326849, DOI: 10.1074/jbc.m114.603977.Peer-Reviewed Original ResearchMeSH Keywords3T3-L1 CellsAcetylationAdipocytesAnimalsBlotting, WesternCarrier ProteinsCell MembraneCells, CulturedCystinyl AminopeptidaseCytoplasmFlow CytometryGlucoseGlucose Transporter Type 4HumansHypoglycemic AgentsImmunoprecipitationInsulinIntracellular Signaling Peptides and ProteinsMaleMiceMice, Inbred C57BLMice, KnockoutProtein TransportReal-Time Polymerase Chain ReactionReverse Transcriptase Polymerase Chain ReactionRNA, MessengerSirtuin 2ConceptsGLUT4 storage vesiclesGLUT4 glucose transportersInsulin-regulated aminopeptidaseGolgin-160Acetylated residuesC-terminusGolgi matrix proteinsSirtuin 2Insulin-responsive vesiclesGlucose transporterUnstimulated cellsGLUT4 traffickingInsulin-stimulated glucose uptakeGlucose uptakeC-terminal peptidePlasma membraneIntracellular compartmentsMatrix proteinsACBD3Protein promotesWild-type controlsDependent deacetylaseGLUT4Proteolytic processingIntracellular retention
2012
Endoproteolytic Cleavage of TUG Protein Regulates GLUT4 Glucose Transporter Translocation*
Bogan JS, Rubin BR, Yu C, Löffler MG, Orme CM, Belman JP, McNally LJ, Hao M, Cresswell JA. Endoproteolytic Cleavage of TUG Protein Regulates GLUT4 Glucose Transporter Translocation*. Journal Of Biological Chemistry 2012, 287: 23932-23947. PMID: 22610098, PMCID: PMC3390669, DOI: 10.1074/jbc.m112.339457.Peer-Reviewed Original Research3T3-L1 CellsAdipocytesAmino Acid SequenceAnimalsCarrier ProteinsGlucoseGlucose Transporter Type 4Golgi ApparatusGreen Fluorescent ProteinsHEK293 CellsHumansImmunoblottingInsulinIntracellular Signaling Peptides and ProteinsMiceMicroscopy, FluorescenceMolecular Sequence DataMutationProtein TransportProteolysisRNA InterferenceSequence Homology, Amino AcidRegulation of Glucose Transporter Translocation in Health and Diabetes
Bogan JS. Regulation of Glucose Transporter Translocation in Health and Diabetes. Annual Review Of Biochemistry 2012, 81: 507-532. PMID: 22482906, DOI: 10.1146/annurev-biochem-060109-094246.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsConceptsTrafficking pathwaysVesicle trafficking pathwaysAS160/TBC1D4GLUT4 glucose transportersGlucose transporter translocationRab GTPasesTrafficking itineraryTransporter translocationIntracellular membranesPlasma membraneInsulin signalingGlucose transporterCell surfaceStorage vesiclesUnstimulated cellsGlucose uptakeTranslocationVesiclesInsulin exposurePathwayFat cellsPathogenesis of diabetesMembraneGTPasesVAMP2
2011
The Ubiquitin Regulatory X (UBX) Domain-containing Protein TUG Regulates the p97 ATPase and Resides at the Endoplasmic Reticulum-Golgi Intermediate Compartment*
Orme CM, Bogan JS. The Ubiquitin Regulatory X (UBX) Domain-containing Protein TUG Regulates the p97 ATPase and Resides at the Endoplasmic Reticulum-Golgi Intermediate Compartment*. Journal Of Biological Chemistry 2011, 287: 6679-6692. PMID: 22207755, PMCID: PMC3307297, DOI: 10.1074/jbc.m111.284232.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesBiological TransportCell Cycle ProteinsEndoplasmic ReticulumGene ExpressionGene Knockdown TechniquesGolgi ApparatusHEK293 CellsHeLa CellsHumansIntracellular Signaling Peptides and ProteinsOncogene Proteins, FusionProtein Structure, QuaternaryProtein Structure, TertiaryProtein TransportUbiquitinValosin Containing ProteinConceptsUBX domainIntermediate compartmentEndoplasmic reticulum-Golgi intermediate compartmentEndoplasmic reticulum exit sitesEarly secretory pathwayGolgi intermediate compartmentATP-bound stateP97/VCPN-terminal domainN-terminal regionP97 hexamerUbiquitylated proteinsHexameric ATPaseUbiquitylated substratesP97 activityCellular processesSecretory pathwayOligomeric statusMembrane fusionC-terminusGolgi complexEndoplasmic reticulumHEK293 cellsCell typesHeLa cellsDual-mode of insulin action controls GLUT4 vesicle exocytosis
Xu Y, Rubin BR, Orme CM, Karpikov A, Yu C, Bogan JS, Toomre DK. Dual-mode of insulin action controls GLUT4 vesicle exocytosis. Journal Of Cell Biology 2011, 193: 643-653. PMID: 21555461, PMCID: PMC3166865, DOI: 10.1083/jcb.201008135.Peer-Reviewed Original ResearchMeSH Keywords3T3-L1 CellsAdipocytesAnimalsBiosensing TechniquesCarrier ProteinsExocytosisGlucose Transporter Type 4Green Fluorescent ProteinsInsulinIntracellular Signaling Peptides and ProteinsKineticsMembrane FusionMiceMicroscopy, FluorescenceMicroscopy, VideoPhospholipase DRecombinant Fusion ProteinsRNA InterferenceTransfectionTransport VesiclesVesicle-Associated Membrane Protein 2ConceptsGLUT4 storage vesiclesVesicle exocytosisInsulin-stimulated control cellsGLUT4 vesicle exocytosisPlasma membrane fusionNovel regulatory siteSingle vesicle exocytosisInsulin triggersVesicle trafficExocytic rateFusion poreSurface of adipocytesMembrane fusionRegulatory sitesPhospholipase DStorage vesiclesPore expansionExocytosisControl cellsAcute perturbationVesiclesInsulin actionVesicle characteristicsAdipocytesCells