2020
Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2
Rampello AJ, Laudermilch E, Vishnoi N, Prophet SM, Shao L, Zhao C, Lusk CP, Schlieker C. Torsin ATPase deficiency leads to defects in nuclear pore biogenesis and sequestration of MLF2. Journal Of Cell Biology 2020, 219: e201910185. PMID: 32342107, PMCID: PMC7265317, DOI: 10.1083/jcb.201910185.Peer-Reviewed Original ResearchConceptsNuclear pore biogenesisMyeloid leukemia factor 2FG nucleoporinsNuclear pore complex biogenesisNuclear envelope herniationsNuclear envelope reformationLive cell imaging platformProteomics-based approachNuclear envelope blebbingComplex biogenesisBleb formationUbiquitin conjugationNuclear envelopeATPase deficiencyBiogenesisHallmark phenotypePhenotypic hallmarksPOM121Factor 2Late markersLuminal componentsNup358CellsUbiquitinBlebbing
2016
Site-specific Proteolysis Mobilizes TorsinA from the Membrane of the Endoplasmic Reticulum (ER) in Response to ER Stress and B Cell Stimulation*
Zhao C, Brown RS, Tang CH, Hu CC, Schlieker C. Site-specific Proteolysis Mobilizes TorsinA from the Membrane of the Endoplasmic Reticulum (ER) in Response to ER Stress and B Cell Stimulation*. Journal Of Biological Chemistry 2016, 291: 9469-9481. PMID: 26953341, PMCID: PMC4850287, DOI: 10.1074/jbc.m115.709337.Peer-Reviewed Original ResearchConceptsEndoplasmic reticulumER stressN-terminal hydrophobic domainHydrophobic domainPrimary cellsPharmacological inhibition profileCell-permeable inhibitorProteolytic cleavage eventsMembrane-associated proteasesTorsin ATPasesATPase familyER membraneDistinct organismsGenetic manipulationCysteine residuesNuclear envelopeCleavage eventsCleavage siteOnly representativeTorsinACell linesReticulumCell stimulationProteaseCells
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