2023
Nuclear envelope assembly relies on CHMP-7 in the absence of BAF–LEM-mediated hole closure
Barger S, Penfield L, Bahmanyar S. Nuclear envelope assembly relies on CHMP-7 in the absence of BAF–LEM-mediated hole closure. Journal Of Cell Science 2023, 136: jcs261385. PMID: 37795681, PMCID: PMC10668030, DOI: 10.1242/jcs.261385.Peer-Reviewed Original ResearchConceptsNuclear envelope assemblySpindle microtubulesNE assemblyEnvelope assemblyC. elegans oocytesLEM-2C. elegansHelix domainBAF-1Family proteinsNucleoplasmic poolNE formationDistinct rolesMicrotubulesAdditional roleNE stabilityPermeability barrierRedundant mechanismsBAFProteinEmbryo survivalBindingAssemblyElegansAutointegrationA membrane-sensing mechanism links lipid metabolism to protein degradation at the nuclear envelope
Lee S, Rodrı́guez J, Merta H, Bahmanyar S. A membrane-sensing mechanism links lipid metabolism to protein degradation at the nuclear envelope. Journal Of Cell Biology 2023, 222: e202304026. PMID: 37382667, PMCID: PMC10309186, DOI: 10.1083/jcb.202304026.Peer-Reviewed Original ResearchMeSH KeywordsAnimalsLipid MetabolismMembrane ProteinsMembranesNuclear EnvelopePhosphoprotein PhosphatasesProteolysisConceptsAmphipathic helixDirect lipid-protein interactionsNuclear envelopeLipid-protein interactionsLipid compositionPhosphatidic acid phosphatase lipin-1INM proteomeNucleoplasmic domainOrganelle identityProteasomal regulationMembrane domainsAnimal cellsProteasomal degradationMaster regulatorProtein degradationLipid environmentLipin-1Packing defectsDAG speciesCTDNEP1Metabolism impactsSUN2Disease mechanismsMetabolismBroad implications
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 ResearchMeSH KeywordsAnimalsCaenorhabditis elegansCell NucleusNuclear EnvelopeNuclear PoreNuclear Pore Complex ProteinsConceptsNuclear pore complexNPC assemblyMembrane biogenesisNE formationNPC densityNuclear pore complex assemblyEndoplasmic reticulumPore complex assemblyNuclear growthPore complexNDC1Redundant rolesComplex assemblyNPC numberBiogenesisMembrane incorporationFast turnoverNuclear formationBilayer lipidsNup53Membrane synthesisFirst divisionAssemblyGrowthNup160
2021
Coupling lipid synthesis with nuclear envelope remodeling
Barger SR, Penfield L, Bahmanyar S. Coupling lipid synthesis with nuclear envelope remodeling. Trends In Biochemical Sciences 2021, 47: 52-65. PMID: 34556392, PMCID: PMC9943564, DOI: 10.1016/j.tibs.2021.08.009.Peer-Reviewed Original ResearchConceptsNuclear envelopeEndoplasmic reticulumNuclear membraneNuclear envelope remodelingLipid-protein interactionsBiosynthesis of lipidsNE remodelingGenome protectionDynamic remodeling processesNE dynamicsLipid speciesCell growthBilayer lipidsLipid synthesisNew roleMembraneLipidsRecent evidenceRemodeling processGenomeRemodelingBiosynthesisProtective barrierSpeciesProtein
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 ResearchMeSH KeywordsAnimalsCell CycleHumansLipid BilayersLipid MetabolismMembrane FusionMitosisNuclear EnvelopeConceptsNuclear 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 compositionMitosisReticulumCompartmentalizationRegulated lipid synthesis and LEM2/CHMP7 jointly control nuclear envelope closure
Penfield L, Shankar R, Szentgyörgyi E, Laffitte A, Mauro MS, Audhya A, Müller-Reichert T, Bahmanyar S. Regulated lipid synthesis and LEM2/CHMP7 jointly control nuclear envelope closure. Journal Of Cell Biology 2020, 219: e201908179. PMID: 32271860, PMCID: PMC7199858, DOI: 10.1083/jcb.201908179.Peer-Reviewed Original ResearchConceptsER membraneNuclear permeability barrierESCRT-III componentsC. elegans oocytesMeiotic spindle microtubulesDe novo glycerolipid synthesisPermeability barrierGlycerolipid synthesisESCRT componentsESCRT-IIIProtein phosphataseCytoplasmic membraneSpindle microtubulesNE permeabilityMeiotic spindleLipid synthesis
2018
The Inner Nuclear Membrane Takes On Lipid Metabolism
Merta H, Bahmanyar S. The Inner Nuclear Membrane Takes On Lipid Metabolism. Developmental Cell 2018, 47: 397-399. PMID: 30458132, DOI: 10.1016/j.devcel.2018.11.005.Peer-Reviewed Original ResearchMeSH KeywordsLipid DropletsLipid MetabolismLipidsMembrane ProteinsNuclear EnvelopeSaccharomyces cerevisiae