2017
Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1
Chase AR, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1. Molecular Biology Of The Cell 2017, 28: 2765-2772. PMID: 28814508, PMCID: PMC5638581, DOI: 10.1091/mbc.e17-05-0281.Peer-Reviewed Original Research
2015
The Torsin Activator LULL1 Is Required for Efficient Growth of Herpes Simplex Virus 1
Turner EM, Brown RS, Laudermilch E, Tsai PL, Schlieker C. The Torsin Activator LULL1 Is Required for Efficient Growth of Herpes Simplex Virus 1. Journal Of Virology 2015, 89: 8444-8452. PMID: 26041288, PMCID: PMC4524217, DOI: 10.1128/jvi.01143-15.Peer-Reviewed Original ResearchConceptsNuclear egressDouble knockout cell linesNuclear envelope dynamicsType II transmembrane proteinHerpes simplex virus 1HSV-1 nuclear egressKnockout cell linesSimplex virus 1Viral protein productionAAA ringGenome engineeringTransmembrane proteinLULL1CRISPR/Virus 1Unexpected roleProtein productionComprehensive geneticPhenotypic analysisHost cellsViral genomeEnvelope dynamicsEfficient growthCell linesHSV-1 production
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
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
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