Evidence map›Paper›PMID 12771384›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2003

RGS3 mediates a calcium-dependent termination of G protein signaling in sensory neurons.

Patrizia Tosetti, Narendra Pathak, Michele H Jacob, Kathleen Dunlap

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
1.1field-weighted citation impact, top 28% 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

11 citing papers in PubMed, 28 citations in OpenAlex.

  1. Article
  2. Article
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  4. A finer tuning of G-protein signaling through regulated control of RGS proteins.American journal of physiology. Heart and circulatory physiology · 2012
    Review
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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

4 authors at 2 institutions in 1 country.

Patrizia TosettiDepartment of Neuroscience, Tufts University School of Medicine and Molecular Cardiology Research Institute, New England Medical Center, Boston, MA 02111, USA.
Narendra Pathak
Michele H Jacob
Kathleen Dunlap
Tufts Medical Center · USTufts University · US

Funding

ULTRASTRUCTURAL ANALYSIS OF NEURONAL SYNAPTIC ANTIGENSR01NS021725 · NINDS · WORCESTER FOUNDATION FOR BIOMEDICAL RES · PI JACOB, MICHELE H. · 1985 to 2009
$2.8M
PRESYNAPTIC RECEPTORS ON SENSORY NEURONSR01NS016483 · NINDS · TUFTS UNIVERSITY BOSTON · PI DUNLAP, KATHLEEN · 1985 to 2007
$2.2M
NINDS NIH HHS NS16483NINDS NIH HHS NS21725NINDS NIH HHS R01 NS016483NINDS NIH HHS R01 NS021725
6 · The paper itself

Abstract

G proteins modulate synaptic transmission. Regulators of G protein signaling (RGS) proteins accelerate the intrinsic GTPase activity of Galpha subunits, and thus terminate G protein activation. Whether RGS proteins themselves are under cellular control is not well defined, particularly in native cells. In dorsal root ganglion neurons overexpressing RGS3, we find that G protein signaling is rapidly terminated (or "desensitized") by calcium influx through voltage-gated channels. This rapid desensitization is most likely mediated by direct binding of calcium to RGS3, as deletion of an EF-hand domain in RGS3 abolishes both the desensitization (observed physiologically) and a calcium-RGS3 interaction (observed in a gel-shift assay). A naturally occurring variant of RGS3 that lacks the EF hand neither binds calcium nor produces rapid desensitization, giving rise instead to a slower calcium-dependent desensitization that is attenuated by a calmodulin antagonist. Thus, activity-evoked calcium entry in sensory neurons may provide differential control of G protein signaling, depending on the isoform of RGS3 expressed in the cells. In complex neural circuits subjected to abundant synaptic inhibition by G proteins (as occurs in dorsal spinal cord), rapid termination of inhibition by electrical activity by EF hand-containing RGS3 may ensure the faithful transmission of information from the most active sensory inputs.

Indexed as

GTPase-Activating ProteinsAnimalsBase SequenceCalcium ChannelsCalcium SignalingChick EmbryoDNA, Complementarygamma-Aminobutyric AcidGanglia, SpinalGenetic VariationGTP-Binding ProteinsNeurons, AfferentProtein Structure, TertiaryRecombinant ProteinsRGS ProteinsSynaptic TransmissionCalcium ChannelsDNA, Complementarygamma-Aminobutyric AcidGTPase-Activating ProteinsGTP-Binding ProteinsRecombinant ProteinsRgs3 protein, mouseRGS Proteins

Identifiers

PMID12771384
PMCPMC165876
OpenAlexW2087713164

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.