2004
Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase
Svedine S, Wang T, Halaban R, Hebert DN. Carbohydrates act as sorting determinants in ER-associated degradation of tyrosinase. Journal Of Cell Science 2004, 117: 2937-2949. PMID: 15161941, DOI: 10.1242/jcs.01154.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCalnexinCarbohydrate MetabolismCells, CulturedEndoplasmic ReticulumEndoplasmic Reticulum Chaperone BiPGlucoseHeat-Shock ProteinsMannoseMelanocytesMiceMolecular ChaperonesMonophenol MonooxygenaseMutationProteasome Endopeptidase ComplexProtein Disulfide-IsomerasesProtein TransportConceptsLectin chaperonesMutant tyrosinaseEndoplasmic reticulum (ER) quality control machineryQuality control machineryProtein disulfide isomeraseDegradation of tyrosinaseERAD substratesChaperone interactionsNon-native substratesER organizationProtein maturationER retentionER lumenDisulfide isomeraseAberrant proteinsProteasomal degradationGlucose trimmingProtein degradationProtein aggregatesTyrosinase degradationSubsequent degradationChaperonesIntact melanocytesMaturation processProteasome
2003
Tyrosinase Maturation and Oligomerization in the Endoplasmic Reticulum Require a Melanocyte-specific Factor*
Francis E, Wang N, Parag H, Halaban R, Hebert DN. Tyrosinase Maturation and Oligomerization in the Endoplasmic Reticulum Require a Melanocyte-specific Factor*. Journal Of Biological Chemistry 2003, 278: 25607-25617. PMID: 12724309, DOI: 10.1074/jbc.m303411200.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCalnexinCalreticulinCells, CulturedCentrifugation, Density GradientCHO CellsCricetinaeCross-Linking ReagentsDimerizationDogsElectrophoresis, Polyacrylamide GelEndoplasmic ReticulumLectinsMelanocytesMembrane GlycoproteinsMiceMicrosomesMonophenol MonooxygenaseMutationOxidoreductasesPancreasPlasmidsPolysaccharidesProtein BindingProtein BiosynthesisProtein FoldingProtein TransportProteinsRabbitsSucroseTime FactorsTranscription, GeneticTrypsinConceptsMelanocyte-specific factorsSemipermeabilized cellsEndoplasmic reticulum retentionLectin chaperones calnexinMelanocyte-specific proteinsTyrosinase-related protein 1Wild-type tyrosinaseSynthesis of melaninChaperone interactionsChaperone calnexinTyrosinase maturationMouse melanocytesTrypsin-resistant stateProtein 1Human tyrosinaseTranslation systemOligomerizationPersistent interactionsMaturationMelanocytesTyrosinaseCellsCalnexinMisfoldingER
2002
Abnormal Acidification of Melanoma Cells Induces Tyrosinase Retention in the Early Secretory Pathway*
Halaban R, Patton RS, Cheng E, Svedine S, Trombetta ES, Wahl ML, Ariyan S, Hebert DN. Abnormal Acidification of Melanoma Cells Induces Tyrosinase Retention in the Early Secretory Pathway*. Journal Of Biological Chemistry 2002, 277: 14821-14828. PMID: 11812790, DOI: 10.1074/jbc.m111497200.Peer-Reviewed Original Research
2000
Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*
Halaban R, Cheng E, Svedine S, Aron R, Hebert D. Proper Folding and Endoplasmic Reticulum to Golgi Transport of Tyrosinase Are Induced by Its Substrates, DOPA and Tyrosine*. Journal Of Biological Chemistry 2000, 276: 11933-11938. PMID: 11124258, DOI: 10.1074/jbc.m008703200.Peer-Reviewed Original ResearchConceptsWild-type tyrosinaseEndoplasmic reticulumProper foldingWild-type proteinMelanoma cellsLoss of pigmentationTyrosinase-positive melanoma cellsGolgi transportType proteinAlbino mutantS proteasomeSubsequent retranslocationMutant formsCatalytic stateEnzymatic activityProteolytic degradationNative formReticulumFoldingProteinTumor-derived antigenic peptidesTyrosinase activitySuppress tyrosinase activityCellsMetabolic changesTranslation Rate of Human Tyrosinase Determines ItsN-Linked Glycosylation Level*
Újvári A, Aron R, Eisenhaure T, Cheng E, Parag H, Smicun Y, Halaban R, Hebert D. Translation Rate of Human Tyrosinase Determines ItsN-Linked Glycosylation Level*. Journal Of Biological Chemistry 2000, 276: 5924-5931. PMID: 11069924, DOI: 10.1074/jbc.m009203200.Peer-Reviewed Original ResearchConceptsTranslation rateCell-free systemProtein translation ratesType I membrane glycoproteinsNormal melanocytesHuman tyrosinaseSemi-permeabilized cellsMelanoma cellsUbiquitin-proteasomal pathwayRate of translationSite-directed mutagenesisWild-type tyrosinaseProtein synthesis inhibitor cycloheximideInefficient glycosylationGlycosylation efficiencyAberrant retentionProtein translationCotranslational eventsConsensus sitesCore glycanDegradative fateProtein doubletEndoplasmic reticulumMaturation eventsAmelanotic melanoma cellsEndoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism
Halaban R, Svedine S, Cheng E, Smicun Y, Aron R, Hebert D. Endoplasmic reticulum retention is a common defect associated with tyrosinase-negative albinism. Proceedings Of The National Academy Of Sciences Of The United States Of America 2000, 97: 5889-5894. PMID: 10823941, PMCID: PMC18529, DOI: 10.1073/pnas.97.11.5889.Peer-Reviewed Original ResearchMeSH KeywordsAlbinism, OculocutaneousAmino Acid SubstitutionAnimalsCalcium-Binding ProteinsCalnexinCalreticulinCells, CulturedEndoplasmic ReticulumGolgi ApparatusHumansMelanocytesMelanosomesMiceMice, Mutant StrainsMicroscopy, FluorescenceMonophenol MonooxygenasePoint MutationProtein BindingProtein FoldingRecombinant Fusion ProteinsRibonucleoproteinsTransfection
1997
Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells
Halaban R, Cheng E, Zhang Y, Moellmann G, Hanlon D, Michalak M, Setaluri V, Hebert D. Aberrant retention of tyrosinase in the endoplasmic reticulum mediates accelerated degradation of the enzyme and contributes to the dedifferentiated phenotype of amelanotic melanoma cells. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 6210-6215. PMID: 9177196, PMCID: PMC21028, DOI: 10.1073/pnas.94.12.6210.Peer-Reviewed Original ResearchMeSH KeywordsAdultCalcium-Binding ProteinsCalnexinCalreticulinCell DifferentiationCells, CulturedCoculture TechniquesEndoplasmic ReticulumEnzyme PrecursorsHumansInfant, NewbornKineticsMelanocytesMelanomaMolecular ChaperonesMolecular WeightMonophenol MonooxygenasePhenotypeRibonucleoproteinsSkin NeoplasmsTime FactorsTumor Cells, CulturedConceptsEndoplasmic reticulumNormal melanocytesER chaperone calnexinMelanin synthesisMalignant melanocytesMelanoma cellsChaperone bindingAberrant retentionChaperone calnexinGolgi compartmentSubcellular localizationAmelanotic melanoma cell lineKey enzymeMelanoma cell linesMaturation of tyrosinaseAmelanotic melanoma cellsKinetics of synthesisInhibitor sensitivityDedifferentiated phenotypeProteolytic degradationCell linesProteasome inhibitorsEnzymeProteasomeImmature forms