ArticleBMC cell biology2012
Palmitoylation and membrane cholesterol stabilize μ-opioid receptor homodimerization and G protein coupling.
Article in BMC cell biology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 103 citations in OpenAlex.
- Effects of Membrane Cholesterol on the Structure and Function of Selected Class A GPCRs─Challenges and Future Perspectives.Biochemistry · 2025Review
- Early Events in βThe Journal of membrane biology · 2024Article
- Lipid regulation of the glucagon receptor family.The Journal of endocrinology · 2024Review
- G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024Review
- The structure of theProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Rafting on the Evidence for Lipid Raft-like Domains as Hubs Triggering Environmental Toxicants' Cellular Effects.Molecules (Basel, Switzerland) · 2023Review
- [Effect ofNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023Article
- Molecular Biophysics of Class A G Protein Coupled Receptors-Lipids Interactome at a Glance-Highlights from the ABiomolecules · 2023Review
- Docking cholesterol to integral membrane proteins with Rosetta.PLoS computational biology · 2023Article
- Ptchd1 mediates opioid tolerance via cholesterol-dependent effects on μ-opioid receptor trafficking.Nature neuroscience · 2022Article
- Dynamic lipid turnover in photoreceptors and retinal pigment epithelium throughout life.Progress in retinal and eye research · 2022Review
- ZDHHC18 negatively regulates cGAS-mediated innate immunity through palmitoylation.The EMBO journal · 2022Article
- Functional expression of opioid receptors and other human GPCRs in yeast engineered to produce human sterols.Nature communications · 2022Article
- Fatty Acids: An Insight into the Pathogenesis of Neurodegenerative Diseases and Therapeutic Potential.International journal of molecular sciences · 2022Review
- Emulating Membrane Protein Environments─How Much Lipid Is Required for a Native Structure: Influenza S31N M2.Journal of the American Chemical Society · 2022Article
- Modulation of Morphine Analgesia, Antinociceptive Tolerance, and Mu-Opioid Receptor Binding by the Cannabinoid CB2 Receptor Agonist O-1966.Frontiers in pharmacology · 2022Article
- Protein Palmitoylation Modification During Viral Infection and Detection Methods of Palmitoylated Proteins.Frontiers in cellular and infection microbiology · 2022Review
- Genetic and functional analysis of a Pacific hagfish opioid system.Journal of neuroscience research · 2022Article
- Novel variants of engineered water soluble mu opioid receptors with extensive mutations and removal of cysteines.Proteins · 2021Article
- Insights into the Role of Membrane Lipids in the Structure, Function and Regulation of Integral Membrane Proteins.International journal of molecular sciences · 2021Review
8 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
backgroundA cholesterol-palmitoyl interaction has been reported to occur in the dimeric interface of the β₂-adrenergic receptor crystal structure. We sought to investigate whether a similar phenomenon could be observed with μ-opioid receptor (OPRM1), and if so, to assess the role of cholesterol in this class of G protein-coupled receptor (GPCR) signaling.
resultsC3.55(170) was determined to be the palmitoylation site of OPRM1. Mutation of this Cys to Ala did not affect the binding of agonists, but attenuated receptor signaling and decreased cholesterol associated with the receptor signaling complex. In addition, both attenuation of receptor palmitoylation (by mutation of C3.55[170] to Ala) and inhibition of cholesterol synthesis (by treating the cells with simvastatin, a HMG-CoA reductase inhibitor) impaired receptor signaling, possibly by decreasing receptor homodimerization and Gαi2 coupling; this was demonstrated by co-immunoprecipitation, immunofluorescence colocalization and fluorescence resonance energy transfer (FRET) analyses. A computational model of the OPRM1 homodimer structure indicated that a specific cholesterol-palmitoyl interaction can facilitate OPRM1 homodimerization at the TMH4-TMH4 interface.
conclusionsWe demonstrate that C3.55(170) is the palmitoylation site of OPRM1 and identify a cholesterol-palmitoyl interaction in the OPRM1 complex. Our findings suggest that this interaction contributes to OPRM1 signaling by facilitating receptor homodimerization and G protein coupling. This conclusion is supported by computational modeling of the OPRM1 homodimer.
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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.