Evidence map›Paper›PMID 16571747›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2006

Synergistic control of protein kinase Cgamma activity by ionotropic and metabotropic glutamate receptor inputs in hippocampal neurons.

Franca Codazzi, Alessandra Di Cesare, Nino Chiulli, Alberto Albanese, Tobias Meyer, Daniele Zacchetti, Fabio Grohovaz

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 34 papers.

0numbers the graph read from it
0cells of the map it votes in
34citing papers in PubMed
2.4field-weighted citation impact, top 12% 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

34 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
  2. Dual Regulation of Spine-Specific and Synapse-to-Nucleus Signaling by PKCδ during Plasticity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023
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  17. M1-muscarinic receptors promote fear memory consolidation via phospholipase C and the M-current.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
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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

7 authors at 5 institutions in 2 countries.

Franca CodazziDepartment of Neuroscience, San Raffaele Scientific Institute, Vita-Salute San Raffaele University, I-20132 Milano, Italy. codazzi.franca@hsr.it
Alessandra Di Cesare
Nino Chiulli
Alberto Albanese
Tobias Meyer
Daniele Zacchetti
Fabio Grohovaz
San Raffaele University of Rome · ITVita-Salute San Raffaele University · ITFondazione IRCCS Istituto Neurologico Carlo Besta · ITIRCCS Ospedale San Raffaele · ITStanford Medicine · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conventional protein kinase C (PKC) isoforms are abundant neuronal signaling proteins with important roles in regulating synaptic plasticity and other neuronal processes. Here, we investigate the role of ionotropic and metabotropic glutamate receptor (iGluR and mGluR, respectively) activation on the generation of Ca2+ and diacylglycerol (DAG) signals and the subsequent activation of the neuron-specific PKCgamma isoform in hippocampal neurons. By combining Ca2+ imaging with total internal reflection microscopy analysis of specific biosensors, we show that elevation of both Ca2+ and DAG is necessary for sustained translocation and activation of EGFP (enhanced green fluorescent protein)-PKCgamma. Both DAG production and PKCgamma translocation were localized processes, typically observed within discrete microdomains along the dendritic branches. Markedly, intermediate-strength NMDA receptor (NMDAR) activation or moderate electrical stimulation generated Ca2+ but no DAG signals, whereas mGluR activation generated DAG but no Ca2+ signals. Both receptors were needed for PKCgamma activation. This suggests that a coincidence detection process exists between iGluRs and mGluRs that relies on a molecular coincidence detection process based on the corequirement of Ca2+ and DAG for PKCgamma activation. Nevertheless, the requirement for costimulation with mGluRs could be overcome for maximal NMDAR stimulation through a direct production of DAG via activation of the Ca2+-sensitive PLCdelta (phospholipase Cdelta) isoform. In a second important exception, mGluRs were sufficient for PKCgamma activation in neurons in which Ca2+ stores were loaded by previous electrical activity. Together, the dual activation requirement for PKCgamma provides a plausible molecular interpretation for different synergistic contributions of mGluRs to long-term potentiation and other synaptic plasticity processes.

Indexed as

AnimalsCalciumCalcium SignalingCells, CulturedDiglyceridesEnzyme ActivationHippocampusNeuronal PlasticityNeuronsProtein Kinase CRatsRats, Sprague-DawleyReceptors, GlutamateReceptors, Metabotropic GlutamateSynaptic TransmissionCalciumDiglyceridesProtein Kinase Cprotein kinase C gammaReceptors, GlutamateReceptors, Metabotropic Glutamate

Identifiers

PMID16571747
PMCPMC6673850
OpenAlexW2027619860

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.