ArticleJournal of lipid research2009
Sphingomyelin synthase SMS2 displays dual activity as ceramide phosphoethanolamine synthase.
Article in Journal of lipid research, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 62 citations in OpenAlex.
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- Acid ceramidase modulates the lipid profile and exacerbates sensitivity to ferroptosis in senescent cells.Research square · 2025Article
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- Cryo-EM structure of human sphingomyelin synthase and its mechanistic implications for sphingomyelin synthesis.Nature structural & molecular biology · 2024Article
- Fine-tuned protein-lipid interactions in biological membranes: exploration and implications of the ORMDL-ceramide negative feedback loop in the endoplasmic reticulum.Frontiers in cell and developmental biology · 2024Article
- Lipidome of theBiochemistry · 2023Article
- Endogenous ceramide phosphoethanolamine modulates circadian rhythm via neural-glial coupling inNational science review · 2022Article
- Human Brain Lipidomics: Pilot Analysis of the Basal Ganglia Sphingolipidome in Parkinson's Disease and Lewy Body Disease.Metabolites · 2022Article
- Sphingomyelin Synthase Family and Phospholipase Cs.Advances in experimental medicine and biology · 2022Article
- Ceramide/Sphingomyelin Rheostat Regulated by Sphingomyelin Synthases and Chronic Diseases in Murine Models.Journal of lipid and atherosclerosis · 2020Review
- Defective cortex glia plasma membrane structure underlies light-induced epilepsy inProceedings of the National Academy of Sciences of the United States of America · 2018Article
- Neuronal Lipid Metabolism: Multiple Pathways Driving Functional Outcomes in Health and Disease.Frontiers in molecular neuroscience · 2018Review
- Possible Role of Phosphatidylcholine and Sphingomyelin on Fumonisin B1-mediated Toxicity.Food safety (Tokyo, Japan) · 2017Review
- Switching head group selectivity in mammalian sphingolipid biosynthesis by active-site-engineering of sphingomyelin synthases.Journal of lipid research · 2017Article
- ER residency of the ceramide phosphoethanolamine synthase SMSr relies on homotypic oligomerization mediated by its SAM domain.Scientific reports · 2017Article
- An inducible ER-Golgi tether facilitates ceramide transport to alleviate lipotoxicity.The Journal of cell biology · 2017Article
- Monitoring Changes in the Oligomeric State of a Candidate Endoplasmic Reticulum (ER) Ceramide Sensor by Single-molecule Photobleaching.The Journal of biological chemistry · 2016Article
- Switching head group selectivity in mammalian sphingolipid biosynthesis by active-site engineering of sphingomyelin synthases.Journal of lipid research · 2016Article
- Article
- DAG tales: the multiple faces of diacylglycerol--stereochemistry, metabolism, and signaling.Cellular and molecular life sciences : CMLS · 2015Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sphingolipids are vital components of eukaryotic membranes involved in the regulation of cell growth, death, intracellular trafficking, and the barrier function of the plasma membrane (PM). While sphingomyelin (SM) is the major sphingolipid in mammals, previous studies indicate that mammalian cells also produce the SM analog ceramide phosphoethanolamine (CPE). Little is known about the biological role of CPE or the enzyme(s) responsible for CPE biosynthesis. SM production is mediated by the SM synthases SMS1 in the Golgi and SMS2 at the PM, while a closely related enzyme, SMSr, has an unknown biochemical function. We now demonstrate that SMS family members display striking differences in substrate specificity, with SMS1 and SMSr being monofunctional enzymes with SM and CPE synthase activity, respectively, and SMS2 acting as a bifunctional enzyme with both SM and CPE synthase activity. In agreement with the PM residency of SMS2, we show that both SM and CPE synthase activities are enhanced at the surface of SMS2-overexpressing HeLa cells. Our findings reveal an unexpected diversity in substrate specificity among SMS family members that should enable the design of specific inhibitors to target the biological role of each enzyme individually.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.