2023
Coordinating nucleoporin condensation and nuclear pore complex assembly
Kuiper E, Prophet S, Schlieker C. Coordinating nucleoporin condensation and nuclear pore complex assembly. FEBS Letters 2023, 597: 2534-2545. PMID: 37620293, DOI: 10.1002/1873-3468.14725.Peer-Reviewed Reviews, Practice Guidelines, Standards, and Consensus StatementsNPC assemblyNuclear pore complexNuclear pore complex assemblyPore complex assemblyAberrant condensationNPC biogenesisAssembly machineryPore complexProtein complexesComplex assemblyRepeat nucleoporinsHuman disordersAmyotrophic lateral sclerosisAssemblyEukaryotesNucleoporinsBiogenesisRibosomesRecent progressProteasomeComplexesLateral sclerosisMachineryHomeostasisTherapeutic interventions
2022
Ndc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth
Mauro MS, Celma G, Zimyanin V, Magaj MM, Gibson KH, Redemann S, Bahmanyar S. Ndc1 drives nuclear pore complex assembly independent of membrane biogenesis to promote nuclear formation and growth. ELife 2022, 11: e75513. PMID: 35852146, PMCID: PMC9296133, DOI: 10.7554/elife.75513.Peer-Reviewed Original ResearchConceptsNuclear pore complexNPC assemblyMembrane biogenesisNE formationNPC densityNuclear pore complex assemblyEndoplasmic reticulumPore complex assemblyNuclear growthPore complexNDC1Redundant rolesComplex assemblyNPC numberBiogenesisMembrane incorporationFast turnoverNuclear formationBilayer lipidsNup53Membrane synthesisFirst divisionAssemblyGrowthNup160p97/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
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
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