ArticleBiochemistry2009
The Gbeta5-RGS7 complex selectively inhibits muscarinic M3 receptor signaling via the interaction between the third intracellular loop of the receptor and the DEP domain of RGS7.
Article in Biochemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- RGS6 regulates Kappa opioid receptor-mediated antinociceptive behaviors.Neuropharmacology · 2026Article
- The association of GNB5 with Alzheimer disease revealed by genomic analysis restricted to variants impacting gene function.American journal of human genetics · 2024Article
- Article
- Subtype-dependent regulation of Gβγ signalling.Cellular signalling · 2021Review
- Structural organization of a major neuronal G protein regulator, the RGS7-Gβ5-R7BP complex.eLife · 2018Article
- The Newly Synthesized Pyrazole Derivative 5-(1-(3 Fluorophenyl)-1Frontiers in physiology · 2018Article
- Regulator of G-protein signaling Gβ5-R7 is a crucial activator of muscarinic M3 receptor-stimulated insulin secretion.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Regulation of neurite morphogenesis by interaction between R7 regulator of G protein signaling complexes and G protein subunit GαThe Journal of biological chemistry · 2017Article
- The evolution of regulators of G protein signalling proteins as drug targets - 20 years in the making: IUPHAR Review 21.British journal of pharmacology · 2017Review
- Article
- Regulator of G Protein Signaling 7 (RGS7) Can Exist in a Homo-oligomeric Form That Is Regulated by Gαo and R7-binding Protein.The Journal of biological chemistry · 2016Article
- Fine Mapping of the Body Fat QTL on Human Chromosome 1q43.PloS one · 2016Article
- Orphan Receptor GPR158 Is an Allosteric Modulator of RGS7 Catalytic Activity with an Essential Role in Dictating Its Expression and Localization in the Brain.The Journal of biological chemistry · 2015Article
- Helix 8 and the i3 loop of the muscarinic M3 receptor are crucial sites for its regulation by the Gβ5-RGS7 complex.Biochemistry · 2015Article
- DEP domains: structurally similar but functionally different.Nature reviews. Molecular cell biology · 2014Review
- Differential effects of the Gβ5-RGS7 complex on muscarinic M3 receptor-induced Ca2+ influx and release.Molecular pharmacology · 2014Article
- Article
- A physiologically required G protein-coupled receptor (GPCR)-regulator of G protein signaling (RGS) interaction that compartmentalizes RGS activity.The Journal of biological chemistry · 2013Article
- Macromolecular composition dictates receptor and G protein selectivity of regulator of G protein signaling (RGS) 7 and 9-2 protein complexes in living cells.The Journal of biological chemistry · 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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2 authors.
Funding
Abstract
Regulators of G protein signaling (RGS) make up a diverse family primarily known as GTPase-activating proteins (GAPs) for heterotrimeric G proteins. In addition to the RGS domain, which is responsible for GAP activity, most RGS proteins contain other distinct structural motifs. For example, members of the R7 family of RGS proteins contain a DEP, GGL, and novel DHEX domain and are obligatory dimers with G protein beta subunit Gbeta5. Here we show that the Gbeta5-RGS7 complex can inhibit Ca2+ mobilization elicited by muscarinic acetylcholine receptor type 3 (M3R), but not by other Gq-coupled receptors such as M1, M5, histamine H1, and GNRH receptors. The isolated DEP domain of RGS7 is sufficient for the inhibition of M3R signaling, whereas the deletion of the DEP domain renders the Gbeta5-RGS7 complex ineffective. Deletion of a portion of the third intracellular loop allowed the receptor (M3R-short) to signal but rendered it insensitive to the effect of the Gbeta5-RGS7 complex. Accordingly, the recombinant DEP domain bound in vitro to the GST-fused i3 loop of the M3R. These results identify a novel molecular mechanism that can impart receptor subtype selectivity on signal transduction via Gq-coupled muscarinic receptors.
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