RGS7 Attenuates Signal Transduction Through the Gαq Family of Heterotrimeric G Proteins in Mammalian Cells

@article{Shuey1998RGS7AS,
  title={RGS7 Attenuates Signal Transduction Through the G$\alpha$q Family of Heterotrimeric G Proteins in Mammalian Cells},
  author={David J. Shuey and M. Kong Betty and P. G. Jones and Xavier Z. Khawaja and Mark I. Cockett},
  journal={Journal of Neurochemistry},
  year={1998},
  volume={70}
}
Abstract: The RGS proteins are a recently discovered family of G protein regulators that have been shown to act as GTPase‐activating proteins (GAPs) on the Gαi and Gαq subfamilies of the heterotrimeric G proteins. Here, we demonstrate that RGS7 is a potent GAP in vitro on Gαi1 and Gαo heterotrimeric proteins and that RGS7 acts to down‐regulate Gαq‐mediated calcium mobilization in a whole‐cell assay system using a transient expression protocol. This RGS protein and RGS4 are reported to be… 
A Novel Kind of G Protein Heterodimer: The Gβ5-RGS Complex
TLDR
The G g 5-RGS interaction has been demonstrated both in vitro and in vivo and has been shown to stabilize the dimer against proteolytic degradation, as well as their posttranslational modifications and localization.
RGS7 and RGS8 Differentially Accelerate G Protein-mediated Modulation of K+ Currents*
TLDR
In situ hybridization study revealed that RGS7 mRNA is predominantly expressed in Golgi cells within granule cell layer of cerebellar cortex and binds preferentially to Gαo, Gαi3, and Gαz, and the acceleration properties of RGS proteins may play important roles in the rapid regulation of neuronal excitability and the cellular responses to short-lived stimulations.
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Abstract: Members of the newly discovered regulator of G protein signaling (RGS) families of proteins have a common RGS domain. This RGS domain is necessary for conferring upon RGS proteins the
Interaction between RGS7 and polycystin.
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    Proceedings of the National Academy of Sciences of the United States of America
  • 1999
TLDR
The identified a short-lived RGS protein, RGS7, that is rapidly degraded through the proteasome pathway and interaction with integral membrane proteins are potential means of regulating RGS proteins.
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TLDR
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TLDR
This review summarizes the current understanding of the biology of the R7 RGS complexes including their structure/functional organization, protein–protein interactions, and physiological roles.
The regulator of G protein signaling family.
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What has been learned so far about the role of RGS proteins in regulating G protein-coupled receptor signaling is discussed and areas that may be fruitful for future research are pointed out.
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TLDR
RGS/β5 complexes may contribute to the selectivity of signal transduction initiated by receptors coupled to Gi and Go by binding to phospholipase C and stimulating the GTPase activity of Gαo.
RGS PROTEINS: INTRODUCTION TO A FAMILY OF GAPS FOR Ga SUBUNITS Regulation of G Protein–Coupled Receptor Signaling
TLDR
What has been learned so far about the role of RGS proteins in regulating G protein–coupled receptor signaling is discussed and areas that may be fruitful for future research are pointed out.
Structure, function, and localization of Gβ5-RGS complexes.
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References

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Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells.
TLDR
It is demonstrated that either of two such RGS proteins, RGS4 or GAIP, attenuated signal transduction mediated by endogenous receptors, G proteins, and effectors when stably expressed as tagged proteins in transfected mammalian cells.
RGS10 is a selective activator of G alpha i GTPase activity.
TLDR
It is demonstrated that RGS proteins can attenuate signalling pathways involving heterotrimeric G proteins by serving as GTPase-activating proteins for specific types of G alpha subunits.
RGS4 and GAIP are GTPase-activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha.
TLDR
It is demonstrated here that two RGS proteins, RGS4 and GAIP, also act as GAPs for Gq alpha, the G alpha protein responsible for activation of phospholipase C beta, and block activation by guanosine 5'-(3-O-thio) triphosphate-Gq alpha.
Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family
TLDR
Introducing RGS family members into yeast blunts signal transduction through the pheromone-response pathway and markedly impair MAP kinase activation by mammalian G-protein-linked receptors, indicating the existence and importance of an SST2-like desensitization mechanism in mammalian cells.
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TLDR
It is reported that RGS (for regulator of G-protein signalling) proteins are GAPs for G alpha subunits, and these RGS proteins are likely to regulate a subset of the G- protein signalling pathways in mammalian cells.
Regulators of G-Protein Signaling (RGS) Proteins: Region-Specific Expression of Nine Subtypes in Rat Brain
TLDR
These results, which document highly specific patterns of RGS mRNA expression in brain and their ability to be regulated in a dynamic manner, support the view that RGS proteins may play an important role in determining the intensity and specificity of signaling pathways in brain as well as their adaptations to synaptic activity.
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TLDR
A potential role for RGS3 is suggested in modulating the LH secretory responsiveness of the pituitary gonadotrope to GnRH by attenuation of Gq alpha protein activation of phospholipase C.
The Aspergillus FlbA RGS domain protein antagonizes G protein signaling to block proliferation and allow development.
TLDR
FlbA's role in modulating the FadA proliferation signal is dependent upon the intrinsic GTPase activity of wild‐type FAdA, and it is proposed that the primary role of FlbA in sporulation is in blocking activation of FADA signaling.
GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of G alpha i subunits.
TLDR
GAIP interacted preferentially with the activated (GTP) form of G alpha i3, which is in keeping with its GAP activity, and is concluded that GAIP is a membrane-anchored GAP with a cysteine string motif.
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