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 ResearchMeSH KeywordsAnimalsEndoplasmic ReticulumHumansMammalsMembrane ProteinsUbiquitinUbiquitin-Conjugating EnzymesUbiquitin-Protein LigasesConceptsProtein 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
2021
Nodal modulator (NOMO) is required to sustain endoplasmic reticulum morphology
Amaya C, Cameron C, Devarkar SC, Seager S, Gerstein MB, Xiong Y, Schlieker C. Nodal modulator (NOMO) is required to sustain endoplasmic reticulum morphology. Journal Of Biological Chemistry 2021, 297: 100937. PMID: 34224731, PMCID: PMC8327139, DOI: 10.1016/j.jbc.2021.100937.Peer-Reviewed Original ResearchMeSH KeywordsAutophagyEndoplasmic ReticulumEndoplasmic Reticulum StressHomeostasisHumansLysosomesProteomicsSequestosome-1 ProteinConceptsEndoplasmic reticulumER structural integrityGenetic epistasis analysisMembrane-bound organellesP62/sequestosome 1Endoplasmic reticulum morphologyImmunoglobulin-like domainsProtein light chain 3Light chain 3Epistasis analysisIdentical orthologsProteomic screenER morphologyHuman genomeMolecular playersNOMO1Protein foldingSequestosome 1Unknown functionER networkChain 3Lipid synthesisProper functionProtein 1Orthologs
2020
The 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 ResearchMeSH KeywordsAnimalsDystoniaEndoplasmic ReticulumHSC70 Heat-Shock ProteinsHumansMolecular ChaperonesNuclear EnvelopeConceptsNuclear 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
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
2013
Arresting a Torsin ATPase Reshapes the Endoplasmic Reticulum*
Rose AE, Zhao C, Turner EM, Steyer AM, Schlieker C. Arresting a Torsin ATPase Reshapes the Endoplasmic Reticulum*. Journal Of Biological Chemistry 2013, 289: 552-564. PMID: 24275647, PMCID: PMC3879577, DOI: 10.1074/jbc.m113.515791.Peer-Reviewed Original ResearchRegulation 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
2011
Enzymatic Blockade of the Ubiquitin-Proteasome Pathway
Ernst R, Claessen JH, Mueller B, Sanyal S, Spooner E, van der Veen AG, Kirak O, Schlieker CD, Weihofen WA, Ploegh HL. Enzymatic Blockade of the Ubiquitin-Proteasome Pathway. PLOS Biology 2011, 8: e1000605. PMID: 21468303, PMCID: PMC3066133, DOI: 10.1371/journal.pbio.1000605.Peer-Reviewed Original Research
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