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
2018
Integration of Biochemical and Mechanical Signals at the Nuclear Periphery: Impacts on Skin Development and Disease
Stewart R, King M, Horsley V. Integration of Biochemical and Mechanical Signals at the Nuclear Periphery: Impacts on Skin Development and Disease. Stem Cell Biology And Regenerative Medicine 2018, 263-292. DOI: 10.1007/978-3-319-16769-5_11.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsNuclear laminaIntegral inner nuclear membrane proteinsInner nuclear membrane proteinSkin developmentMechanical signalsNuclear membrane proteinsInner nuclear membraneIntegration of biochemicalGenome integrityNuclear peripheryTranscriptional outputNuclear laminsAssociated chromatinMembrane proteinsNuclear interiorTissue-level mechanicsGene expressionNuclear membraneSkin homeostasisKeratinocyte differentiationMechanical inputChromatinLaminsLaminaProteinThe Molecular Composition and Function of the Nuclear Periphery and Its Impact on the Genome
Lusk C, King M. The Molecular Composition and Function of the Nuclear Periphery and Its Impact on the Genome. 2018, 35-62. DOI: 10.1007/978-3-319-71614-5_2.Peer-Reviewed Original ResearchNuclear peripheryNuclear subcompartmentsIntegral inner nuclear membrane proteinsInner nuclear membrane proteinSpecific genic regionsRepressive histone marksNuclear membrane proteinsGene-poor chromatinModern genomic analysesGenome stabilityHistone marksNuclear architectureGenic regionsTranscriptional outputNuclear laminsGene positionMembrane proteinsGenomic analysisDevelopmental inputsMolecular insightsMolecular componentsGenomeModel systemMolecular compositionCurrent understanding
2016
Cooperative Activity of GABP with PU.1 or C/EBPε Regulates Lamin B Receptor Gene Expression, Implicating Their Roles in Granulocyte Nuclear Maturation
Malu K, Garhwal R, Pelletier MG, Gotur D, Halene S, Zwerger M, Yang ZF, Rosmarin AG, Gaines P. Cooperative Activity of GABP with PU.1 or C/EBPε Regulates Lamin B Receptor Gene Expression, Implicating Their Roles in Granulocyte Nuclear Maturation. The Journal Of Immunology 2016, 197: 910-922. PMID: 27342846, PMCID: PMC5022553, DOI: 10.4049/jimmunol.1402285.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsCCAAT-Enhancer-Binding ProteinsCell DifferentiationCell NucleusChromatin ImmunoprecipitationElectrophoretic Mobility Shift AssayGA-Binding Protein Transcription FactorGene Expression RegulationGranulocytesHEK293 CellsHematopoietic Stem CellsHumansImmunoblottingMiceMice, Inbred C57BLMutagenesis, Site-DirectedProto-Oncogene ProteinsReal-Time Polymerase Chain ReactionReceptors, Cytoplasmic and NuclearSignal TransductionTrans-ActivatorsConceptsLamin B receptorTranscription factorsGene expressionInner nuclear membrane proteinNuclear membrane proteinsFamily transcription factorsNuclear envelope proteinsETS transcription factorsExpression of genesRole of ETSTranscriptional regulatorsTranscriptional activationCombinatorial actionMembrane proteinsLBR geneEts siteEarly myeloid progenitorsCCAAT enhancerGABPSuch cooperative interactionsNeutrophil differentiationGenesMyeloid progenitorsReceptor gene expressionPromoter
2014
Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4
Webster BM, Colombi P, Jäger J, Lusk CP. Surveillance of Nuclear Pore Complex Assembly by ESCRT-III/Vps4. Cell 2014, 159: 388-401. PMID: 25303532, PMCID: PMC4194032, DOI: 10.1016/j.cell.2014.09.012.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyNuclear compartmentalizationIntegral inner nuclear membrane proteinsESCRT-III/Vps4Functional nuclear pore complexesNuclear pore complex assemblyInner nuclear membrane proteinPore complex assemblyNuclear membrane proteinsAAA ATPase Vps4LEM familyPore complexAssembly intermediatesMembrane proteinsLoss of compartmentalizationComplex assemblyNuclear envelopeComplex compartmentVps4CompartmentalizationCell functionContinuum of mechanismsAssemblySnf7
2008
A Network of Nuclear Envelope Membrane Proteins Linking Centromeres to Microtubules
King MC, Drivas TG, Blobel G. A Network of Nuclear Envelope Membrane Proteins Linking Centromeres to Microtubules. Cell 2008, 134: 427-438. PMID: 18692466, PMCID: PMC2617791, DOI: 10.1016/j.cell.2008.06.022.Peer-Reviewed Original ResearchConceptsSUN-KASH complexesNuclear membrane proteinsMembrane proteinsIntegral inner nuclear membrane proteinsSUN domain protein Sad1Nuclear envelopeSpindle pole body componentInner nuclear membrane proteinFission yeast S. pombeOuter nuclear membrane proteinsCytoplasmic microtubulesYeast S. pombeMicrotubule-dependent forcesNuclear envelope membranesCentromeric DNAS. pombeCentromeric heterochromatinHeterochromatic regionsEnvelope membraneIMA1MicrotubulesSad1HeterochromatinProteinNuclear heterochromatin
2006
Karyopherin-mediated import of integral inner nuclear membrane proteins
King MC, Lusk C, Blobel G. Karyopherin-mediated import of integral inner nuclear membrane proteins. Nature 2006, 442: 1003-1007. PMID: 16929305, DOI: 10.1038/nature05075.Peer-Reviewed Original ResearchConceptsIntegral membrane proteinsInner nuclear membraneINM proteinsMembrane proteinsIntegral inner nuclear membrane proteinsInner nuclear membrane proteinNuclear pore complex proteinsNuclear membrane proteinsRan GTPase cycleBasic sequence motifsNuclear localization signalNuclear pore complexPore complex proteinsAppropriate cellular compartmentDiscrete sequence elementsINM targetingLocalization signalPore complexGTPase cycleNuclear transportSequence motifsCellular compartmentsComplex proteinsSequence elementsKaryopherin β1
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