2024
Structure and mechanism of the human CTDNEP1–NEP1R1 membrane protein phosphatase complex necessary to maintain ER membrane morphology
Gao S, Rodríguez J, Bahmanyar S, Airola M. Structure and mechanism of the human CTDNEP1–NEP1R1 membrane protein phosphatase complex necessary to maintain ER membrane morphology. Proceedings Of The National Academy Of Sciences Of The United States Of America 2024, 121: e2321167121. PMID: 38776370, PMCID: PMC11145253, DOI: 10.1073/pnas.2321167121.Peer-Reviewed Original ResearchConceptsProtein phosphatase complexPhosphatase complexER membrane biogenesisHigh-resolution crystal structuresProtein serine/threonine phosphatasesCancer-associated mutationsDevelopment of medulloblastomaMembrane biogenesisSubstrate recognitionER expansionActive siteRegulatory subunitSubstrate peptideMammalian cellsSerine/threonine phosphataseIdentical phenotypesArg residuesMolecular detailsSubunit 1Phosphatase 1Inactivating mutationsPeptide sequencesAggressive childhood cancerMutationsPhosphatase activity
2021
Cell cycle regulation of ER membrane biogenesis protects against chromosome missegregation
Merta H, Carrasquillo Rodríguez JW, Anjur-Dietrich MI, Vitale T, Granade ME, Harris TE, Needleman DJ, Bahmanyar S. Cell cycle regulation of ER membrane biogenesis protects against chromosome missegregation. Developmental Cell 2021, 56: 3364-3379.e10. PMID: 34852214, PMCID: PMC8692360, DOI: 10.1016/j.devcel.2021.11.009.Peer-Reviewed Original ResearchConceptsChromosome missegregationEndoplasmic reticulumLipin-1Accurate chromosome segregationER membrane biogenesisCell cycle regulationPhosphatidic acid phosphatase lipin-1Chromosome segregationMembrane biogenesisER membraneChromosome movementMitotic fidelityCycle regulationER sizeMitosis resultsMitotic cytoplasmFormation of micronucleiMitotic cellsMitotic errorsMissegregationER reorganizationHuman cellsBiophysical propertiesCancer cellsLipid metabolism
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 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