ArticleScientific reports2016
Binding Characteristics of Sphingosine-1-Phosphate to ApoM hints to Assisted Release Mechanism via the ApoM Calyx-Opening.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 27 citations in OpenAlex.
- Plasma apoM and S1P levels are inversely associated with mortality in African Americans with type 2 diabetes mellitus.Journal of lipid research · 2019Trial
- Molecular characteristics of apolipoprotein M and its biological functions in kidney diseases.Molecular and cellular biochemistry · 2026Review
- Apolipoprotein M: Structural insights, functional roles, and therapeutic approaches in vascular disease.The Journal of biological chemistry · 2026Review
- Apolipoprotein M expression modifies the sphingolipid landscape in murine blood and lymph.Frontiers in immunology · 2025Article
- Unbiased MD simulations identify lipid binding sites in lipid transfer proteins.The Journal of cell biology · 2024Article
- Designer high-density lipoprotein particles enhance endothelial barrier function and suppress inflammation.Science signaling · 2024Article
- Hepatic FoxOs link insulin signaling with plasma lipoprotein metabolism through an apolipoprotein M/sphingosine-1-phosphate pathway.The Journal of clinical investigation · 2022Article
- Structural basis of sphingosine-1-phosphate receptor 1 activation and biased agonism.Nature chemical biology · 2022Article
- Glycation of HDL Polymerizes Apolipoprotein M and Attenuates Its Capacity to Bind to Sphingosine 1-Phosphate.Journal of atherosclerosis and thrombosis · 2021Article
- Serum Sphingosine-1-Phosphate Is Decreased in Patients With Acute-on-Chronic Liver Failure and Predicts Early Mortality.Hepatology communications · 2020Article
- A conformation-specific ON-switch for controlling CAR T cells with an orally available drug.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Sphingosine 1-Phosphate in Malaria Pathogenesis and Its Implication in Therapeutic Opportunities.Frontiers in cellular and infection microbiology · 2020Review
- Review
- Sphingosine 1-phosphate and inflammation.International immunology · 2019Review
- 'Crystal' Clear? Lysophospholipid Receptor Structure Insights and Controversies.Trends in pharmacological sciences · 2018Review
- Divergent Role of Sphingosine 1-Phosphate in Liver Health and Disease.International journal of molecular sciences · 2018Review
- Sphingosine kinase and sphingosine-1-phosphate in liver pathobiology.Critical reviews in biochemistry and molecular biology · 2017Review
- A Novel Perspective on the ApoM-S1P Axis, Highlighting the Metabolism of ApoM and Its Role in Liver Fibrosis and Neuroinflammation.International journal of molecular sciences · 2017Review
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Sphingosine-1-phosphate (S1P) is a lysophospholipid mediator carried by the HDL-associated apoM protein in blood, regulating many physiological processes by activating the G protein-coupled S1P receptor in mammals. Despite the solved crystal structure of the apoM-S1P complex, the mechanism of S1P release from apoM as a part of the S1P pathway is unknown. Here, the dynamics of the wild type apoM-S1P complex as well as of mutants were investigated by means of atomistic molecular dynamics simulations. The potential of mean force for S1P unbinding from apoM reflected a large binding strength of more than 60 kJ/mol. This high unbinding free energy for S1P underlines the observed specificity of the physiological effects of S1P as it suggests that the spontaneous release of S1P from apoM is unlikely. Instead, S1P release and thus the control of this bioactive lipid probably requires the tight interaction with other molecules, e.g. with the S1P receptor. Mutations of specific S1P anchoring residues of apoM decreased the energetic barrier by up to 20 kJ/mol. Moreover, the ligand-free apoM protein is shown to adopt a more open upper hydrophilic binding pocket and to result in complete closure of the lower hydrophobic cavity, suggesting a mechanism for adjusting the gate for ligand access.
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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.