ArticleNature communications2023
Structural basis for catalysis of human choline/ethanolamine phosphotransferase 1.
Article in Nature communications, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 43 citations in OpenAlex.
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- Membrane Fusion-Inspired Nanomaterials: Emerging Strategies for Infectious Disease and Cancer Diagnostics.Advanced healthcare materials · 2026Review
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- Effects of Dietary Garlic Skin Based on Metabolomics Analysis in the Meat Quality of Black Goats.Foods (Basel, Switzerland) · 2025Article
- Structural basis for catalysis and selectivity of phospholipid synthesis by eukaryotic choline-phosphotransferase.Nature communications · 2025Article
- Cellular and organismal function of choline metabolism.Nature metabolism · 2025Review
- The study of the relationship between food additives and the childhood asthma based on metabolome analysis.Frontiers in immunology · 2025Article
- Advancing Anticancer Drug Discovery: Leveraging Metabolomics and Machine Learning for Mode of Action Prediction by Pattern Recognition.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
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- Innovations in Antifungal Drug Discovery among Cell Envelope Synthesis Enzymes through Structural Insights.Journal of fungi (Basel, Switzerland) · 2024Review
- Architects of the membrane: structures of eukaryotic choline phosphotransferase 1 and choline/ethanolamine phosphotransferase 1.Nature structural & molecular biology · 2023Article
- The effects of Phycocyanobilin on experimental arthritis involve the reduction in nociception and synovial neutrophil infiltration, inhibition of cytokine production, and modulation of the neuronal proteome.Frontiers in immunology · 2023Article
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Phosphatidylcholine (PC) and phosphatidylethanolamine (PE) are two primary components of the eukaryotic membrane and play essential roles in the maintenance of membrane integrity, lipid droplet biogenesis, autophagosome formation, and lipoprotein formation and secretion. Choline/ethanolamine phosphotransferase 1 (CEPT1) catalyzes the last step of the biosynthesis of PC and PE in the Kennedy pathway by transferring the substituted phosphate group from CDP-choline/ethanolamine to diacylglycerol. Here, we present the cryo-EM structures of human CEPT1 and its complex with CDP-choline at resolutions of 3.7 Å and 3.8 Å, respectively. CEPT1 is a dimer with 10 transmembrane segments (TMs) in each protomer. TMs 1-6 constitute a conserved catalytic domain with an interior hydrophobic chamber accommodating a PC-like density. Structural observations and biochemical characterizations suggest that the hydrophobic chamber coordinates the acyl tails during the catalytic process. The PC-like density disappears in the structure of the complex with CDP-choline, suggesting a potential substrate-triggered product release mechanism.
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