Control of calcium oscillations by phosphorylation of metabotropic glutamate receptors

@article{Kawabata1996ControlOC,
  title={Control of calcium oscillations by phosphorylation of metabotropic glutamate receptors},
  author={Shigeki Kawabata and Rie Tsutsumi and Atsuyuki Kohara and Tokio Yamaguchi and Shigetada Nakanishi and Masamichi Okada},
  journal={Nature},
  year={1996},
  volume={383},
  pages={89-92}
}
STIMULATION of two metabotropic glutamate-receptor subtypes, mGluRl and mGluRS, triggers the release of Ca2+ from intra-cellular stores through the inositol-(1,4,5) trisphosphate (InsP3) pathway1,3. Here we report that glutamate induces single-peaked intracellular Ca2+ mobilization in mGluR1α-transfected cells but elicits Ca2+ oscillations in mGluRSa-transfected cells. The response patterns of the intracellular Ca2+ increase depend upon the identity of a single amino acid, aspartate (at… 
Diversity of Calcium Signaling by Metabotropic Glutamate Receptors*
TLDR
The results provide a novel concept in which oscillatory/non-oscillatory mobilizations of Ca2+ induce different coupling mechanisms during prolonged stimulation of mGluRs.
Determinants of Metabotropic Glutamate Receptor-5-mediated Ca2+ and Inositol 1,4,5-Trisphosphate Oscillation Frequency
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A single receptor can stimulate two types of InsP3-mediated Ca2+ signal dependent upon feedback inhibition, producing two distinct means of controlling the final pattern of Ca2- i release.
Effects of Positive Allosteric Modulators on Single-Cell Oscillatory Ca2+ Signaling Initiated by the Type 5 Metabotropic Glutamate Receptor
TLDR
It is demonstrated that allosteric modulators can “tune” the Ca2+ oscillation frequency initiated by mGlu5 receptor activation, and this might allow pharmacological modification of the downstream processes (e.g., transcriptional regulation) that is unachievable through orthosteric ligand interactions.
Calmodulin dynamically regulates the trafficking of the metabotropic glutamate receptor mGluR5
TLDR
Calmodulin (CaM) is identified as a dynamic regulator of mGluR5 trafficking and phosphorylation of serine 901 (S901) is demonstrated, thereby directly linking PKC phosphorylated, CaM binding, receptor trafficking, and downstream signaling.
cAMP-Dependent Protein Kinase Inhibits mGluR2 Coupling to G-Proteins by Direct Receptor Phosphorylation
TLDR
Forskolin has a similar inhibitory effect on putative mGluR2-mediated responses at the medial perforant path synapse and that this effect of forskolin is blocked by a selective inhibitor of cAMP-dependent protein kinase (PKA).
Metabotropic glutamate receptor 5 and calcium signaling in retinal amacrine cells
TLDR
Results indicate that GABAergic amacrine cells express an avian version of mGluR5 that is linked to phospholipase C‐dependent Ca2+ release and Ca2- influx, possibly through TRP channels.
Altered Expression of Gq/11α Protein Shapes mGlu1 and mGlu5 Receptor-Mediated Single Cell Inositol 1,4,5-Trisphosphate and Ca2+ Signaling
TLDR
It is indicated that altering Gq/11α expression levels differentially affects spatiotemporal aspects of IP3 and Ca2+ signaling mediated by the mGlu1/5 receptor-mediated IP2+ signals, using RNA interference.
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. Duvoisin
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences of the United States of America
  • 2000
TLDR
Evidence is provided for a differential regulation by PKC and protein kinase A of two distinct mGluR1alpha-dependent signaling pathways and 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.
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