ArticleMolecular and cellular biology2011
β-arrestin2 plays permissive roles in the inhibitory activities of RGS9-2 on G protein-coupled receptors by maintaining RGS9-2 in the open conformation.
Article in Molecular and cellular biology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 34 citations in OpenAlex.
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- Unveiling the Differences in Signaling and Regulatory Mechanisms between Dopamine DInternational journal of molecular sciences · 2023Review
- RGS9-2 rescues dopamine D2 receptor levels and signaling inEMBO molecular medicine · 2019Article
- Design, synthesis, and evaluation of bitopic arylpiperazine-phthalimides as selective dopamine DMedChemComm · 2018Article
- Regulation of neurite morphogenesis by interaction between R7 regulator of G protein signaling complexes and G protein subunit GαThe Journal of biological chemistry · 2017Article
- Molecular Signature That Determines the Acute Tolerance of G Protein-Coupled Receptors.Biomolecules & therapeutics · 2017Article
- RGS2 modulates the activity and internalization of dopamine D2 receptors in neuroblastoma N2A cells.Neuropharmacology · 2016Article
- Functional Regulation of Dopamine D₃ Receptor through Interaction with PICK1.Biomolecules & therapeutics · 2016Article
- Roles of Dopamine D₂ Receptor Subregions in Interactions with β-Arrestin2.Biomolecules & therapeutics · 2016Article
- Moderate Alcohol Exposure during the Rat Equivalent to the Third Trimester of Human Pregnancy Alters Regulation of GABAA Receptor-Mediated Synaptic Transmission by Dopamine in the Basolateral Amygdala.Frontiers in pediatrics · 2014Article
- Novel roles for β-arrestins in the regulation of pharmacological sequestration to predict agonist-induced desensitization of dopamine D3 receptors.British journal of pharmacology · 2013Article
- GIRK channel modulation by assembly with allosterically regulated RGS proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
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Abstract
Together with G protein-coupled receptor (GPCR) kinases (GRKs) and β-arrestins, RGS proteins are the major family of molecules that control the signaling of GPCRs. The expression pattern of one of these RGS family members, RGS9-2, coincides with that of the dopamine D(3) receptor (D(3)R) in the brain, and in vivo studies have shown that RGS9-2 regulates the signaling of D2-like receptors. In this study, β-arrestin2 was found to be required for scaffolding of the intricate interactions among the dishevelled-EGL10-pleckstrin (DEP) domain of RGS9-2, Gβ5, R7-binding protein (R7BP), and D(3)R. The DEP domain of RGS9-2, under the permission of β-arrestin2, inhibited the signaling of D(3)R in collaboration with Gβ5. β-Arrestin2 competed with R7BP and Gβ5 so that RGS9-2 is placed in the cytosolic region in an open conformation which is able to inhibit the signaling of GPCRs. The affinity of the receptor protein for β-arrestin2 was a critical factor that determined the selectivity of RGS9-2 for the receptor it regulates. These results show that β-arrestins function not only as mediators of receptor-G protein uncoupling and initiators of receptor endocytosis but also as scaffolding proteins that control and coordinate the inhibitory effects of RGS proteins on the signaling of certain GPCRs.
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