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
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
2008
A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway
Schlieker CD, Van der Veen AG, Damon JR, Spooner E, Ploegh HL. A functional proteomics approach links the ubiquitin-related modifier Urm1 to a tRNA modification pathway. Proceedings Of The National Academy Of Sciences Of The United States Of America 2008, 105: 18255-18260. PMID: 19017811, PMCID: PMC2584574, DOI: 10.1073/pnas.0808756105.Peer-Reviewed Original Research
2007
Structure 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