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 transporter
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 role
2015
Acetylation 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 cells