ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2013
The σ-1 receptor interacts directly with GluN1 but not GluN2A in the GluN1/GluN2A NMDA receptor.
Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 87 citations in OpenAlex.
- Review
- Effects of fenfluramine and sigma-1-dependent pharmacological and genetic modulation in a mouse kindling model.Epilepsia · 2026Article
- Sigma receptor ligands in selected affective disorders, psychoses, and addictions - a narrative review.Pharmacological reports : PR · 2026Review
- Organelle contact sites in cancer cells.Cell death & disease · 2026Review
- Targeting Sigma-1 and Sigma-2 Receptors in Neuropathic Pain: Pharmacology, Ligand Development, and Translational Progress.Brain sciences · 2026Review
- Mutated sigma-1R disrupts cell homeostasis in dHMN patient cells.Cellular and molecular life sciences : CMLS · 2025Article
- The sigma-1 receptor as a neurohomeostatic decision hub for GABARAP-mediated receptor trafficking and macroautophagy.Frontiers in molecular biosciences · 2025Article
- Preclinical Evaluation of Sigma 1 Receptor Antagonists as a Novel Treatment for Painful Diabetic Neuropathy.ACS pharmacology & translational science · 2024Article
- Discovery of AD258 as a Sigma Receptor Ligand with Potent Antiallodynic Activity.Journal of medicinal chemistry · 2023Article
- Pharmacological Analysis of GABAInternational journal of molecular sciences · 2023Article
- Synthesis, Computational Insights, and Evaluation of Novel Sigma Receptors Ligands.ACS chemical neuroscience · 2023Article
- Sigma-1 receptor and seizures.Pharmacological research · 2023Review
- Sigma-1 Receptor Signaling: In Search of New Therapeutic Alternatives for Cardiovascular and Renal Diseases.International journal of molecular sciences · 2023Review
- Defining the ligand-dependent proximatome of the sigma 1 receptor.Frontiers in cell and developmental biology · 2023Article
- Sigma-1 Receptors in Depression: Mechanism and Therapeutic Development.Frontiers in pharmacology · 2022Review
- Regulation of membrane NMDA receptors by dynamics and protein interactions.The Journal of cell biology · 2021Review
- Sigma-1 Receptor: A Potential Therapeutic Target for Traumatic Brain Injury.Frontiers in cellular neuroscience · 2021Review
- Deferred Administration of Afobazole Induces Sigma1R-Dependent Restoration of Striatal Dopamine Content in a Mouse Model of Parkinson's Disease.International journal of molecular sciences · 2020Article
- Chaperone Sigma1R and Antidepressant Effect.International journal of molecular sciences · 2020Review
- Contribution of Lysosome and Sigma Receptors to Neuroprotective Effects of Memantine Against Beta-Amyloid in the SH-SY5Y Cells.Advanced pharmaceutical bulletin · 2020Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The σ-1 receptor (Sig1R) is widely expressed in the CNS, where it has a neuroprotective role in ischemia and stroke and an involvement in schizophrenia. The Sig1R interacts functionally with a variety of ion channels, including the NMDA receptor (NMDAR). Here, we used atomic force microscopy (AFM) imaging to investigate the interaction between the Sig1R and the NMDAR. The Sig1R bound directly to GluN1/GluN2A NMDAR heterotetramers. Furthermore, the mean angle between pairs of bound Sig1Rs was 72°. This result suggested that the Sig1R interacts with either GluN1 or GluN2A, but not both, and supports our recent demonstration that the NMDAR subunits adopt an adjacent (i.e., 1/1/2/2) arrangement. The Sig1R could be coisolated with GluN1 but not with GluN2A, indicating that GluN1 is its specific target within the NMDAR. Consistent with this conclusion, AFM imaging of coisolated Sig1R and GluN1 revealed GluN1 dimers decorated with Sig1Rs. In situ proximity ligation assays demonstrated that the Sig1R interacts with GluN1 (but not with GluN2A) within intact cells and also that its C terminus is extracellular. We conclude that the Sig1R binds to the GluN1/GluN2A NMDAR specifically via the GluN1 subunit. This interaction likely accounts for at least some of the modulatory effects of Sig1R ligands on the NMDAR.
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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.