ArticleThe Biochemical journal2002
RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain.
Article in The Biochemical journal, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
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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
15 citing papers in PubMed, 55 citations in OpenAlex.
- 14-3-3γ binds regulator of G protein signaling 14 (RGS14) at distinct sites to inhibit the RGS14:GαThe Journal of biological chemistry · 2018Article
- Regulation of tyrosine hydroxylase is preserved across different homo- and heterodimeric 14-3-3 proteins.Amino acids · 2016Article
- RGS3 controls T lymphocyte migration in a model of Th2-mediated airway inflammation.American journal of physiology. Lung cellular and molecular physiology · 2013Article
- A finer tuning of G-protein signaling through regulated control of RGS proteins.American journal of physiology. Heart and circulatory physiology · 2012Review
- Structural basis for the 14-3-3 protein-dependent inhibition of the regulator of G protein signaling 3 (RGS3) function.The Journal of biological chemistry · 2011Article
- Regulators of G-protein signaling in the heart and their potential as therapeutic targets.Circulation research · 2011Review
- IQGAP1 is a novel CXCR2-interacting protein and essential component of the "chemosynapse".PloS one · 2011Article
- Phosphorylation of myocardin by extracellular signal-regulated kinase.The Journal of biological chemistry · 2009Article
- Pro- and anti-apoptotic dual functions of the C5a receptor: involvement of regulator of G protein signaling 3 and extracellular signal-regulated kinase.Laboratory investigation; a journal of technical methods and pathology · 2009Article
- Regulation of Smad-mediated gene transcription by RGS3.Molecular pharmacology · 2008Article
- R4 RGS proteins: regulation of G-protein signaling and beyond.Pharmacology & therapeutics · 2007Review
- How regulators of G protein signaling achieve selective regulation.Journal of molecular biology · 2007Review
- Psychostimulants, madness, memory... and RGS proteins?Neuromolecular medicine · 2005Review
- Fractalkine (CX3CL1) stimulated by nuclear factor kappaB (NF-kappaB)-dependent inflammatory signals induces aortic smooth muscle cell proliferation through an autocrine pathway.The Biochemical journal · 2003Article
- The 14-3-3 protein as a novel regulator of ion channel localisation.The Journal of physiology · 2002Article
Corrections and comments
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Authors and funding
11 authors at 4 institutions in 1 country.
Funding
Abstract
RGS3 belongs to a family of the regulators of G-protein signalling (RGS), which bind and inhibit the G alpha subunits of heterotrimeric G-proteins via a homologous RGS domain. Increasing evidence suggests that RGS proteins can also interact with targets other than G-proteins. Employing yeast two-hybrid screening of a cDNA library, we identified an interaction between RGS3 and the phosphoserine-binding protein 14-3-3. This interaction was confirmed by in vitro binding and co-immunoprecipitation experiments. RGS3-deletion analysis revealed the presence of a single 14-3-3-binding site located outside of the RGS domain. Ser(264) was then identified as the 14-3-3-binding site of RGS3. The S(264)A mutation resulted in the loss of RGS3 binding to 14-3-3, without affecting its ability to bind G alpha(q). Signalling studies showed that the S(264)A mutant was more potent than the wild-type RGS3 in inhibition of G-protein-mediated signalling. Binding experiments revealed that RGS3 exists in two separate pools, either 14-3-3-bound or G-protein-bound, and that the 14-3-3-bound RGS3 is unable to interact with G-proteins. These data are consistent with the model wherein 14-3-3 serves as a scavenger of RGS3, regulating the amounts of RGS3 available for binding G-proteins. This study describes a new level in the regulation of G-protein signalling, in which the inhibitors of G-proteins, RGS proteins, can themselves be regulated by phosphorylation and binding 14-3-3.
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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.