ArticleBiochimica et biophysica acta. Molecular and cell biology of lipids2021
Sphingomyelin synthase related protein is a mammalian phosphatidylethanolamine phospholipase C.
Article in Biochimica et biophysica acta. Molecular and cell biology of lipids, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed, 15 citations in OpenAlex.
- Sphingolipids in human disease: organ-specific pathologies, chain-length-dependent effects, and translational implications.Journal of translational medicine · 2026Review
- From Classical to Alternative Pathways of 2-Arachidonoylglycerol Synthesis: AlterAGs at the Crossroad of Endocannabinoid and Lysophospholipid Signaling.Molecules (Basel, Switzerland) · 2024Review
- Cryo-EM structure of human sphingomyelin synthase and its mechanistic implications for sphingomyelin synthesis.Nature structural & molecular biology · 2024Article
- Normal and Dysregulated Sphingolipid Metabolism: Contributions to Podocyte Injury and Beyond.Cells · 2024Review
- Review
- Sphingomyelin Synthase Family and Phospholipase Cs.Advances in experimental medicine and biology · 2022Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Sphingomyelin synthase related protein (SMSr) has no SM synthase activity but has ceramide phosphorylethanolamine (CPE) synthase activity in vitro. Although SMSr is ubiquitously expressed in all tested tissues, the CPE levels in most mammalian tissues or cells are extremely low or undetectable. Therefore, SMSr seems not to be a functional CPE synthase in vivo and its real biological function needs to be elucidated. In this study, we utilized purified recombinant SMSr and adenovirus-mediated SMSr in vivo expression to show that SMSr has phosphatidylethanolamine phospholipases C (PE-PLC) activity, i.e., it can generate DAG through PE hydrolysis in the absence of ceramide. Further, we found that SMSr has no phosphatidylcholine (PC)-PLC, phosphatidylserine (PS)-PLC, phosphatidylglycerol (PG)-PLC, and phosphatidic phosphatase (PAP) activities, indicating that SMSr-mediated PE-PLC activity has specificity. We conclude that SMSr is a mammalian PE-PLC. Importantly, SMSr can regulate steady state levels of PE in vivo, and it should be a new tool for PE-related biological study.
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Registered trials
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