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 ResearchMeSH KeywordsCrystallography, X-RayEndoplasmic ReticulumHumansIntracellular MembranesMembrane ProteinsPhosphoprotein PhosphatasesProtein BindingConceptsProtein 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
2023
A 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
2020
Regulated 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