ArticleThe Journal of biological chemistry2011
Type 5 G protein beta subunit (Gbeta5) controls the interaction of regulator of G protein signaling 9 (RGS9) with membrane anchors.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
20 citing papers in PubMed, 26 citations in OpenAlex.
- Genome-Wide Protein Interaction Analysis in Parasitic Gyrodactylus Flatworms-Fish Hosts System and Drug Target Identification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Unveiling the Differences in Signaling and Regulatory Mechanisms between Dopamine DInternational journal of molecular sciences · 2023Review
- Article
- RGS9-2 rescues dopamine D2 receptor levels and signaling inEMBO molecular medicine · 2019Article
- Structural organization of a major neuronal G protein regulator, the RGS7-Gβ5-R7BP complex.eLife · 2018Article
- GNB5 mutation causes a novel neuropsychiatric disorder featuring attention deficit hyperactivity disorder, severely impaired language development and normal cognition.Genome biology · 2016Article
- 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
- Cellular and Subcellular Localization of the RGS7/Gβ5/R7BP Complex in the Cerebellar Cortex.Frontiers in neuroanatomy · 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
- RGS9-2 modulates sensory and mood related symptoms of neuropathic pain.Neurobiology of learning and memory · 2014Article
- Nucleus accumbens-specific interventions in RGS9-2 activity modulate responses to morphine.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2014Article
- DEP domains: structurally similar but functionally different.Nature reviews. Molecular cell biology · 2014Review
- Article
- Article
- Article
- GIRK channel modulation by assembly with allosterically regulated RGS proteins.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- D(2)-Dopamine receptors target regulator of G protein signaling 9-2 to detergent-resistant membrane fractions.Journal of neurochemistry · 2012Article
- 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.Molecular and cellular biology · 2011Article
- Membrane attachment is key to protecting transducin GTPase-activating complex from intracellular proteolysis in photoreceptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2011Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The R7 family of regulators of G protein signaling (RGS) proteins, comprising RGS6, RGS7, RGS9, and RGS11, regulate neuronal G protein signaling pathways. All members of the R7 RGS form trimeric complexes with the atypical G protein β subunit, Gβ5, and membrane anchor R7BP or R9AP. Association with Gβ5 and membrane anchors has been shown to be critical for maintaining proteolytic stability of the R7 RGS proteins. However, despite its functional importance, the mechanism of how R7 RGS forms complexes with Gβ5 and membrane anchors remains poorly understood. Here, we used protein-protein interaction, co-localization, and protein stability assays to show that association of RGS9 with membrane anchors requires Gβ5. We further establish that the recruitment of R7BP to the complex requires an intact interface between the N-terminal lobe of RGS9 and protein interaction surface of Gβ5. Site-directed mutational analysis reveals that distinct molecular determinants in the interface between Gβ5 and N-terminal Dishevelled, EGL-10, Pleckstrin/DEP Helical Extension (DEP/DHEY) domains are differentially involved in R7BP binding and proteolytic stabilization. On the basis of these findings, we conclude that Gβ5 contributes to the formation of the binding site to the membrane anchors and thus is playing a central role in the assembly of the proteolytically stable trimeric complex and its correct localization in the cell.
Indexed as
Identifiers
What OpenQuestion holds
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.