Evidence map›Paper›PMID 26655302›Full record

ReviewMolecular pharmacology2016

Roles for Regulator of G Protein Signaling Proteins in Synaptic Signaling and Plasticity.

Kyle J Gerber, Katherine E Squires, John R Hepler

Open access · bronzeAbstract readReview
In one paragraph

Review in Molecular pharmacology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 75 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
75citing papers in PubMed, 1 pooled it
4.2field-weighted citation impact, top 5% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

75 citing papers in PubMed, 1 synthesis or guideline pooled it, 119 citations in OpenAlex.

  1. Pooled it
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15 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 1 institution in 1 country.

Kyle J GerberPrograms in Molecular and Systems Pharmacology (K.J.G., K.E.S., J.R.H.) and Neuroscience (J.R.H.), Department of Pharmacology (K.J.G., K.E.S., J.R.H.), Emory University School of Medicine, Atlanta, Georgia.
Katherine E SquiresPrograms in Molecular and Systems Pharmacology (K.J.G., K.E.S., J.R.H.) and Neuroscience (J.R.H.), Department of Pharmacology (K.J.G., K.E.S., J.R.H.), Emory University School of Medicine, Atlanta, Georgia.
John R HeplerPrograms in Molecular and Systems Pharmacology (K.J.G., K.E.S., J.R.H.) and Neuroscience (J.R.H.), Department of Pharmacology (K.J.G., K.E.S., J.R.H.), Emory University School of Medicine, Atlanta, Georgia jhepler@emory.edu.
Emory University · US

Funding

Structure and Function of the G-alpha-i1:RGS14:H-Ras signaling complexR01NS037112 · NINDS · EMORY UNIVERSITY · PI HEPLER, JOHN R · 1998 to 2023
$7.2M
Graduate Training in the Pharmacological StudiesT32GM008602 · NIGMS · EMORY UNIVERSITY · PI HALL, RANDY A. · 1996 to 2021
$5.1M
Decoding the RGS14 Interactome/Signalosome in CA2 hippocampal neuronsR21NS087488 · NINDS · EMORY UNIVERSITY · PI HEPLER, JOHN R · 2015 to 2016
$426k
NIGMS NIH HHS T32 GM008602NINDS NIH HHS 1R21NS087488NINDS NIH HHS R01 NS037112NINDS NIH HHS R01NS37112NINDS NIH HHS R21 NS087488
6 · The paper itself

Abstract

The regulator of G protein signaling (RGS) family of proteins serves critical roles in G protein-coupled receptor (GPCR) and heterotrimeric G protein signal transduction. RGS proteins are best understood as negative regulators of GPCR/G protein signaling. They achieve this by acting as GTPase activating proteins (GAPs) for Gα subunits and accelerating the turnoff of G protein signaling. Many RGS proteins also bind additional signaling partners that either regulate their functions or enable them to regulate other important signaling events. At neuronal synapses, GPCRs, G proteins, and RGS proteins work in coordination to regulate key aspects of neurotransmitter release, synaptic transmission, and synaptic plasticity, which are necessary for central nervous system physiology and behavior. Accumulating evidence has revealed key roles for specific RGS proteins in multiple signaling pathways at neuronal synapses, regulating both pre- and postsynaptic signaling events and synaptic plasticity. Here, we review and highlight the current knowledge of specific RGS proteins (RGS2, RGS4, RGS7, RGS9-2, and RGS14) that have been clearly demonstrated to serve critical roles in modulating synaptic signaling and plasticity throughout the brain, and we consider their potential as future therapeutic targets.

Indexed as

AnimalsHumansNeuronal PlasticityReceptors, G-Protein-CoupledRGS ProteinsSignal TransductionReceptors, G-Protein-CoupledRGS Proteins

Identifiers

PMID26655302
PMCPMC4727123
OpenAlexW2277442753

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.