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
2018
Dynamic nanoscale morphology of the ER surveyed by STED microscopy
Schroeder LK, Barentine AES, Merta H, Schweighofer S, Zhang Y, Baddeley D, Bewersdorf J, Bahmanyar S. Dynamic nanoscale morphology of the ER surveyed by STED microscopy. Journal Of Cell Biology 2018, 218: 83-96. PMID: 30442642, PMCID: PMC6314542, DOI: 10.1083/jcb.201809107.Peer-Reviewed Original Research