2022
Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteins
Tsai P, Cameron C, Forni M, Wasko R, Naughton B, Horsley V, Gerstein M, Schlieker C. Dynamic quality control machinery that operates across compartmental borders mediates the degradation of mammalian nuclear membrane proteins. Cell Reports 2022, 41: 111675. PMID: 36417855, PMCID: PMC9827541, DOI: 10.1016/j.celrep.2022.111675.Peer-Reviewed Original ResearchConceptsProtein turnoverCellular quality control systemNuclear membrane proteinsQuality control machineryDistinct cellular compartmentsNuclear envelope proteinsGenetic screenProtein homeostasisUbiquitin ligasesControl machineryMembrane proteinsCellular compartmentsEnzyme Ube2g2Quality control systemEndoplasmic reticulumHuman diseasesEfficient biosynthesisHRD1RNF5Disease variantsTMEM33Envelope proteinSubstrate levelsDisease etiologyModel substrate
2020
Lipid and protein dynamics that shape nuclear envelope identity
Bahmanyar S, Schlieker C. Lipid and protein dynamics that shape nuclear envelope identity. Molecular Biology Of The Cell 2020, 31: 1315-1323. PMID: 32530796, PMCID: PMC7353140, DOI: 10.1091/mbc.e18-10-0636.Peer-Reviewed Original ResearchConceptsNuclear envelopeEndoplasmic reticulumMembrane fusionNuclear pore complex biogenesisUnique protein compositionBulk endoplasmic reticulumDe novo lipid synthesisNPC biogenesisComplex biogenesisNovo lipid synthesisLipid asymmetryProtein dynamicsProtein compositionElusive mechanismLipid synthesisLipid bilayersBiogenesisPermeability barrierFunctional specializationMajor threatLipid metabolismUnique compositionMitosisReticulumCompartmentalizationThe Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease
Rampello AJ, Prophet SM, Schlieker C. The Role of Torsin AAA+ Proteins in Preserving Nuclear Envelope Integrity and Safeguarding Against Disease. Biomolecules 2020, 10: 468. PMID: 32204310, PMCID: PMC7175109, DOI: 10.3390/biom10030468.Peer-Reviewed Original ResearchConceptsNuclear envelopeNuclear pore complex biogenesisEssential cellular processesNormal cellular physiologyNuclear envelope integrityDistinct subcellular localizationEndoplasmic reticulum networkCellular lipid metabolismTorsin ATPasesComplex biogenesisEnvelope integrityRegulatory cofactorsCellular physiologyCellular processesLuminal domainSubcellular localizationConsiderable medical importancePhenotypic consequencesCofactor assemblyTorsinsNE defectsATP hydrolysisReticulum networkDiverse processesPolypeptide 1
2019
An unbiased approach de-livers unexpected insight into torsin biology
Prophet SM, Schlieker C. An unbiased approach de-livers unexpected insight into torsin biology. Journal Of Clinical Investigation 2019, 129: 4576-4579. PMID: 31589164, PMCID: PMC6819095, DOI: 10.1172/jci132442.Peer-Reviewed Original ResearchConceptsFatty liver diseaseHepatic lipid metabolismLiver diseaseNonneural tissuesLipid metabolismBrain functionConditional deletionCongenital disorderDisease etiologySecretion defectHuman pathologiesMammalian liverPolypeptide 1Future investigationsSteatohepatitisUnbiased approachDysfunctionVLDLEtiologyMutationsDiseaseMiceLiverNeuronsPathologyMethodologies to monitor protein turnover at the inner nuclear membrane
Tsai PL, Zhao C, Schlieker C. Methodologies to monitor protein turnover at the inner nuclear membrane. Methods In Enzymology 2019, 619: 47-69. PMID: 30910029, PMCID: PMC6457266, DOI: 10.1016/bs.mie.2018.12.033.Peer-Reviewed Original ResearchConceptsLamin B receptorNuclear envelopeInner nuclear membrane proteinProtein turnoverProtein quality control pathwaysNuclear membrane proteinsQuality control pathwaysProtein turnover machineryHuman congenital disordersInner nuclear membraneSubcellular fractionation methodMammalian nuclear envelopeLive-cell imagingC-terminal truncationsNuclear laminaMembrane proteinsModel substrateBiochemical approachesNuclear compartmentActivity essentialControl pathwaysNuclear membraneRapid turnoverCholesterol biosynthesisCell imaging
2015
A designed repeat protein as an affinity capture reagent.
Speltz EB, Brown RS, Hajare HS, Schlieker C, Regan L. A designed repeat protein as an affinity capture reagent. Biochemical Society Transactions 2015, 43: 874-80. PMID: 26517897, PMCID: PMC5683849, DOI: 10.1042/bst20150091.Peer-Reviewed Original ResearchConceptsProtein-peptide interactionsAffinity capture reagentsSupramolecular arraysNovel reagentCapture reagentPractical applicationsReagentsProtein engineeringGeneral utilityAffinity purificationRational fashionProtein interactionsAttractive targetInteractionImportant practical applicationsPurification
2012
A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation
Sehrawat S, Koenig PA, Kirak O, Schlieker C, Fankhauser M, Ploegh HL. A catalytically inactive mutant of the deubiquitylase YOD-1 enhances antigen cross-presentation. Blood 2012, 121: 1145-1156. PMID: 23243279, PMCID: PMC3575758, DOI: 10.1182/blood-2012-08-447409.Peer-Reviewed Original ResearchMeSH KeywordsAdoptive TransferAnimalsAntigen-Presenting CellsATP Binding Cassette Transporter, Subfamily B, Member 2ATP-Binding Cassette TransportersBrefeldin ACD8-Positive T-LymphocytesCross-PrimingFemaleHydrogen-Ion ConcentrationImmunizationMaleMiceMice, Inbred C57BLMice, KnockoutMice, TransgenicMutation, MissenseOvalbuminPeptide FragmentsRhadinovirusUbiquitin ThiolesteraseConceptsAntigen presenting cellsT cellsPresent exogenous antigensRecombinant herpes virusT cell responsesExogenous antigensPresenting cellsSIINFEKL peptideRecombinant influenzaAntigen processingInclusion of inhibitorsEnhanced expansionMHV-68AntigenImmunizationInfectionVirusCellsCrosspresentationImproved controlInfluenzaMiceSIINFEKL
2007
A Functional Ubiquitin-Specific Protease Embedded in the Large Tegument Protein (ORF64) of Murine Gammaherpesvirus 68 Is Active during the Course of Infection
Gredmark S, Schlieker C, Quesada V, Spooner E, Ploegh HL. A Functional Ubiquitin-Specific Protease Embedded in the Large Tegument Protein (ORF64) of Murine Gammaherpesvirus 68 Is Active during the Course of Infection. Journal Of Virology 2007, 81: 10300-10309. PMID: 17634221, PMCID: PMC2045495, DOI: 10.1128/jvi.01149-07.Peer-Reviewed Original ResearchConceptsLarge tegument proteinTegument proteinsMHV-68-infected cellsCysteine protease domainUbiquitin-specific proteaseAmino-terminal segmentActive site-directed probesActivity-based profilingDeubiquitinating proteaseEnzymatic functionSite-directed probesProtease domainBetaherpesvirus familyProteinORF64Murine gammaherpesvirus 68Tandem mass spectrometryProteaseGammaherpesvirus 68Course of infectionMass spectrometryHerpes simplex virus type 1Simplex virus type 1CellsUL36