2018
Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases
Chase A, Laudermilch E, Wang J, Shigematsu H, Yokoyama T, Schlieker C. Dynamic functional assembly of the Torsin AAA+ ATPase and its modulation by LAP1: a novel mode of regulation for AAA+ ATPases. The FASEB Journal 2018, 32: 114.1-114.1. DOI: 10.1096/fasebj.2018.32.1_supplement.114.1.Peer-Reviewed Original ResearchOligomeric stateNuclear envelope defectsRobust ATPase activityExperimental Biology 2018 MeetingPresence of ATPEnvelope defectsCofactor assemblyHomotypic oligomersCellular cofactorsATP hydrolysisDynamic assemblyFunctional assemblyMolecular etiologyATPase activationLAP1Novel modeATPase activityCofactorFASEB JournalATPasesCofactor systemATPaseAssemblyDYT1 dystoniaKey role
2016
Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study
Laudermilch E, Tsai PL, Graham M, Turner E, Zhao C, Schlieker C. Dissecting Torsin/cofactor function at the nuclear envelope: a genetic study. Molecular Biology Of The Cell 2016, 27: 3964-3971. PMID: 27798237, PMCID: PMC5156537, DOI: 10.1091/mbc.e16-07-0511.Peer-Reviewed Original ResearchConceptsTorsin ATPasesNuclear envelopeNuclear pore complex biogenesisComplex biogenesisRegulatory cofactorsValuable experimental platformHuman genomeCRISPR/Observed phenotypeGenetic studiesFunctional linkATPasesCofactor functionElectron microscopy tomographyImmunogold labelingPhenotypic measuresCell linesCofactor systemBleb structuresBleb formationTOR2ANucleoporinsLULL1BiogenesisGenome
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