Evidence map›Paper›PMID 10823959›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Opposing effects of protein kinase C and protein kinase A on metabotropic glutamate receptor signaling: selective desensitization of the inositol trisphosphate/Ca2+ pathway by phosphorylation of the receptor-G protein-coupling domain.

A Francesconi, R M Duvoisin

Abstract readComparative Study
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 papers.

0numbers the graph read from it
0cells of the map it votes in
44citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

44 citing papers in PubMed, 115 citations in OpenAlex.

  1. Review
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  3. Review
  4. SLC26A3 (DRA) is stimulated in a synergistic, intracellular CaAmerican journal of physiology. Cell physiology · 2023
    Article
  5. Article
  6. mGluR5 in amygdala modulates fear memory generalization.Frontiers in behavioral neuroscience · 2023
    Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. A Critical Role for Sorting Nexin 1 in the Trafficking of Metabotropic Glutamate Receptors.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  12. Metabotropic glutamate receptor trafficking.Molecular and cellular neurosciences · 2018
    Review
  13. Article
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  18. 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

2 authors at 1 institution in 1 country.

A FrancesconiDepartment of Ophthalmology, Margaret M. Dyson Vision Research Institute, Weill Medical College of Cornell University, 1300 York Avenue, New York, NY 10021, USA. afrance@med.cornell.edu
R M Duvoisin
Cornell University · US

Funding

MOLECULAR MECHANISMS OF SIGNAL TRANSDUCTION IN RETINAR01EY009534 · NEI · WEILL MEDICAL COLLEGE OF CORNELL UNIV · PI DUVOISIN, ROBERT M · 1992 to 2010
$2.8M
NEI NIH HHS EY09534NEI NIH HHS R01 EY009534
6 · The paper itself

Abstract

Signaling by the metabotropic glutamate receptor 1alpha (mGluR1alpha) can lead to the accumulation of inositol 1,4, 5-trisphosphate (InsP(3)) and cAMP and to the modulation of K(+) and Ca(2+) channel opening. At present, very little is known about how these different actions are integrated and eventually turned off. Unraveling the molecular mechanisms underlying these functions is crucial for understanding mGluR-mediated regulation of synaptic transmission. It has been shown that receptor-induced activation of the InsP(3) pathway is subject to feedback inhibition mediated by protein kinase C (PKC). In this study, we provide evidence for a differential regulation by PKC and protein kinase A of two distinct mGluR1alpha-dependent signaling pathways. PKC activation selectively inhibits agonist-dependent stimulation of the InsP(3) pathway but does not affect receptor signaling via cAMP. In contrast, protein kinase A potentiates agonist-independent signaling of the receptor via InsP(3). Furthermore, we demonstrate that the selectivity of PKC action on receptor signaling rests on phosphorylation of a threonine residue located in the G protein-interacting domain of the receptor. Modification at Thr(695) selectively disrupts mGluR1alpha-G(q/11) interaction without affecting signaling through G(s). Together, these data provide insight on the mechanisms by which selective down-regulation of a specific receptor-dependent signaling pathway can be achieved and on how cross-talk between different second messenger cascades may contribute to fine-tune short- and long-term receptor activity.

Indexed as

Protein Processing, Post-TranslationalAllosteric RegulationAmino Acid SequenceAnimalsCalcium SignalingCyclic AMPCyclic AMP-Dependent Protein KinasesHeterotrimeric GTP-Binding ProteinsInositol 1,4,5-TrisphosphateIon TransportMolecular Sequence DataOocytesPatch-Clamp TechniquesPhosphorylationPhosphothreonineProtein Kinase CCyclic AMPCyclic AMP-Dependent Protein KinasesHeterotrimeric GTP-Binding ProteinsInositol 1,4,5-TrisphosphatePhosphothreonineProtein Kinase CReceptors, Metabotropic GlutamateRecombinant Fusion Proteins

Identifiers

PMID10823959
PMCPMC18579
OpenAlexW1965058020

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.