2020
Lipid and protein dynamics that shape nuclear envelope identity
Bahmanyar S, Schlieker C. Lipid and protein dynamics that shape nuclear envelope identity. Molecular Biology Of The Cell 2020, 31: 1315-1323. PMID: 32530796, PMCID: PMC7353140, DOI: 10.1091/mbc.e18-10-0636.Peer-Reviewed Original ResearchConceptsNuclear envelopeEndoplasmic reticulumMembrane fusionNuclear pore complex biogenesisUnique protein compositionBulk endoplasmic reticulumDe novo lipid synthesisNPC biogenesisComplex biogenesisNovo lipid synthesisLipid asymmetryProtein dynamicsProtein compositionElusive mechanismLipid synthesisLipid bilayersBiogenesisPermeability barrierFunctional specializationMajor threatLipid metabolismUnique compositionMitosisReticulumCompartmentalizationTorsin 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 componentsNup358CellsUbiquitinBlebbingThe 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 ResearchConceptsNuclear 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
2019
Methodologies to monitor protein turnover at the inner nuclear membrane
Tsai PL, Zhao C, Schlieker C. Methodologies to monitor protein turnover at the inner nuclear membrane. Methods In Enzymology 2019, 619: 47-69. PMID: 30910029, PMCID: PMC6457266, DOI: 10.1016/bs.mie.2018.12.033.Peer-Reviewed Original ResearchConceptsLamin B receptorNuclear envelopeInner nuclear membrane proteinProtein turnoverProtein quality control pathwaysNuclear membrane proteinsQuality control pathwaysProtein turnover machineryHuman congenital disordersInner nuclear membraneSubcellular fractionation methodMammalian nuclear envelopeLive-cell imagingC-terminal truncationsNuclear laminaMembrane proteinsModel substrateBiochemical approachesNuclear compartmentActivity essentialControl pathwaysNuclear membraneRapid turnoverCholesterol biosynthesisCell imaging
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 formationTOR2ANucleoporinsLULL1BiogenesisGenomeSite-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
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