ArticleJournal of neurochemistry2012
D(2)-Dopamine receptors target regulator of G protein signaling 9-2 to detergent-resistant membrane fractions.
Article in Journal of neurochemistry, 2012. 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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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- Cryo-EM structure of human class C orphan GPCR GPR179 involved in visual processing.Nature communications · 2024Article
- A neurodevelopmental disorder mutation locks G proteins in the transitory pre-activated state.Nature communications · 2024Article
- G Protein-Coupled Receptor Dimerization-What Next?International journal of molecular sciences · 2024Review
- Orphan receptor GPR158 serves as a metabotropic glycine receptor: mGlyR.Science (New York, N.Y.) · 2023Article
- The critical balance between dopamine D2 receptor and RGS for the sensitive detection of a transient decay in dopamine signal.PLoS computational biology · 2021Article
- Triple-Knockout, Synuclein-Free Mice Display Compromised Lipid Pattern.Molecules (Basel, Switzerland) · 2021Article
- Gαo is a major determinant of cAMP signaling in the pathophysiology of movement disorders.Cell reports · 2021Article
- Anaplastic Lymphoma Kinase Regulates Internalization of the Dopamine D2 Receptor.Molecular pharmacology · 2020Article
- The differential actions of clozapine and other antipsychotic drugs on the translocation of dopamine D2 receptors to the cell surface.The Journal of biological chemistry · 2019Article
- RGS9-2 rescues dopamine D2 receptor levels and signaling inEMBO molecular medicine · 2019Article
- Regulation of monoamine transporters and receptors by lipid microdomains: implications for depression.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2018Review
- Desensitized D2 autoreceptors are resistant to trafficking.Scientific reports · 2017Article
- Pathways of polyunsaturated fatty acid utilization: implications for brain function in neuropsychiatric health and disease.Brain research · 2015Review
- Role for Rab10 in Methamphetamine-Induced Behavior.PloS one · 2015Article
- Article
- Brain human monoclonal autoantibody from sydenham chorea targets dopaminergic neurons in transgenic mice and signals dopamine D2 receptor: implications in human disease.Journal of immunology (Baltimore, Md. : 1950) · 2013Article
- D1-D2 dopamine receptor synergy promotes calcium signaling via multiple mechanisms.Molecular pharmacology · 2013Article
- Plasma membrane compartmentalization of D2 dopamine receptors.The Journal of biological chemistry · 2013Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Detergent-resistant membranes (DRM) are thought to contain structures such as lipid rafts that are involved in compartmentalizing cell membranes. We report that the majority of D(2)-dopamine receptors (D(2)R) expressed endogenously in mouse striatum or expressed in immortalized cell-lines is found in DRM. In addition, exogenous co-expression of D(2)R in a cell line shifted the expression of regulator of G protein signaling 9-2 (RGS9-2) into DRM. RGS9-2 is a protein that is highly enriched in the striatum and specifically regulates striatal D(2)R. In the striatum, RGS9-2 is mostly associated with DRMs but when expressed in cell lines, RGS9-2 is present in the soluble cytoplasmic fraction. In contrast, the majority of mu opioid receptors and delta opioid receptors are found in detergent-soluble membrane and there was no shift of RGS9-2 into DRM after co-expression of mu opioid receptor. These data suggest that the targeting of RGS9-2 to DRM in the striatum is mediated by D(2)R and that DRM is involved in the formation of a D(2)R signaling complex. D(2)R-mediated targeting of RGS9-2 to DRM was blocked by the deletion of the RGS9-2 DEP domain or by a point mutation that abolishes the GTPase accelerating protein function of RGS9-2.
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Registered trials
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.