2024
Protein folding and quality control during nuclear transport
Mallik S, Poch D, Burick S, Schlieker C. Protein folding and quality control during nuclear transport. Current Opinion In Cell Biology 2024, 90: 102407. PMID: 39142062, DOI: 10.1016/j.ceb.2024.102407.Peer-Reviewed Original ResearchProtein foldingNuclear transportCo-translational transportProtein-folding environmentAggregation of folding intermediatesProtein quality controlNuclear import machineryNuclear pore complexFolding environmentImport machineryNuclear importCytosolic aggregatesContext of neurological disordersNuclear compartmentPore complexProtein synthesisProteinQuality controlFoldingBarrier functionEvolution of transport systemsKaryopherinNucleoporinsCompartmentTemporal coordination
2022
p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells
Prophet SM, Naughton BS, Schlieker C. p97/UBXD1 Generate Ubiquitylated Proteins That Are Sequestered into Nuclear Envelope Herniations in Torsin-Deficient Cells. International Journal Of Molecular Sciences 2022, 23: 4627. PMID: 35563018, PMCID: PMC9100061, DOI: 10.3390/ijms23094627.Peer-Reviewed Original ResearchConceptsUbiquitylated proteinsNuclear pore complex assemblyPore complex assemblyNuclear envelope herniationsP97-dependent mannerP97 activityFG nucleoporinsComplex assemblyATPase deficiencyFG-NupsHeat shockHallmark phenotypeDYT1 dystoniaProteinAberrant depositionP97Therapeutic developmentDisease modelsUBXD1UbiquitylationBlebsK48UbiquitinHeterodimersUnexplored potential
2014
The mechanism of Torsin ATPase activation
Brown RS, Zhao C, Chase AR, Wang J, Schlieker C. The mechanism of Torsin ATPase activation. Proceedings Of The National Academy Of Sciences Of The United States Of America 2014, 111: e4822-e4831. PMID: 25352667, PMCID: PMC4234599, DOI: 10.1073/pnas.1415271111.Peer-Reviewed Original Research
2013
Regulation of Torsin ATPases by LAP1 and LULL1
Zhao C, Brown RS, Chase AR, Eisele MR, Schlieker C. Regulation of Torsin ATPases by LAP1 and LULL1. Proceedings Of The National Academy Of Sciences Of The United States Of America 2013, 110: e1545-e1554. PMID: 23569223, PMCID: PMC3637692, DOI: 10.1073/pnas.1300676110.Peer-Reviewed Original ResearchConceptsType II transmembrane proteinATP-bound stateTorsin ATPasesActivator functionLuminal domainTransmembrane proteinATP hydrolysisNuclear envelopeLULL1Endoplasmic reticulumAutosomal dominant movement disorderTorsinALAP1Activation mechanismATPase activityDistinct fashionFunction mechanismCongenital disorderMutantsATPasesCofactorProteinReticulumATPaseRegulation
2009
The Otubain YOD1 Is a Deubiquitinating Enzyme that Associates with p97 to Facilitate Protein Dislocation from the ER
Ernst R, Mueller B, Ploegh HL, Schlieker C. The Otubain YOD1 Is a Deubiquitinating Enzyme that Associates with p97 to Facilitate Protein Dislocation from the ER. Molecular Cell 2009, 36: 28-38. PMID: 19818707, PMCID: PMC2774717, DOI: 10.1016/j.molcel.2009.09.016.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAlpha 1-AntitrypsinCarrier ProteinsCatalytic DomainCell Cycle ProteinsCell LineEndopeptidasesEndoplasmic ReticulumHumansMembrane ProteinsPoint MutationProteasome Endopeptidase ComplexProtein BindingProtein FoldingProtein Interaction Domains and MotifsProtein TransportReceptors, Antigen, T-Cell, alpha-betaThiolester HydrolasesTransfectionUbiquitinUbiquitinationValosin Containing ProteinZinc FingersConceptsZinc finger domainOvarian tumor (OTU) familyDominant negative effectMisfolded proteinsMultiprotein complexesFinger domainMammalian cellsDislocation substratesProtein dislocationC-terminusEndoplasmic reticulumFunctional linkYOD1P97Core domainEnzymeUbxTumor familyTerminusCytosolDomainProteinReticulumPathwayRole
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 1CellsUL36Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes
Schlieker C, Weihofen WA, Frijns E, Kattenhorn LM, Gaudet R, Ploegh HL. Structure of a Herpesvirus-Encoded Cysteine Protease Reveals a Unique Class of Deubiquitinating Enzymes. Molecular Cell 2007, 25: 677-687. PMID: 17349955, PMCID: PMC7110467, DOI: 10.1016/j.molcel.2007.01.033.Peer-Reviewed Original ResearchConceptsDeubiquitinating enzymePapain-like foldCysteine protease domainLarge tegument proteinActive site cysteineActive site residuesBeta-hairpin loopExtensive hydrophobic interactionsSuicide substrateProtease moduleProtease domainTegument proteinsCysteine proteasesHairpin loopEnzymeThioether linkageUbUnique classHydrophobic interactionsMurine cytomegalovirusUbiquitinDomainProteinMembersCrystal structure