2024
UBXN9 governs GLUT4-mediated spatial confinement of RIG-I-like receptors and signaling
Harrison A, Yang D, Cahoon J, Geng T, Cao Z, Karginov T, Hu Y, Li X, Chiari C, Qyang Y, Vella A, Fan Z, Vanaja S, Rathinam V, Witczak C, Bogan J, Wang P. UBXN9 governs GLUT4-mediated spatial confinement of RIG-I-like receptors and signaling. Nature Immunology 2024, 25: 2234-2246. PMID: 39567760, DOI: 10.1038/s41590-024-02004-7.Peer-Reviewed Original Research
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
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
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 Acid
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