Interactions of the C Terminus of Metabotropic Glutamate Receptor Type 1α with Rat Brain Proteins

@article{Ciruela1999InteractionsOT,
  title={Interactions of the C Terminus of Metabotropic Glutamate Receptor Type 1$\alpha$ with Rat Brain Proteins},
  author={Francisco Ciruela and Melanie J. Robbins and Antony C. Willis and R. A. J. Mcilhinney},
  journal={Journal of Neurochemistry},
  year={1999},
  volume={72}
}
Abstract : Metabotropic glutamate receptors (mGluRs) are coupled to G protein second messenger pathways and modulate glutamate neurotransmission in the brain, where they are targeted to specific synaptic locations. As part of a strategy for defining the mechanisms for the specific targeting of mGluR1 α, rat brain proteins which interact with the intracellular carboxy terminus of mGluR1 α have been characterized, using affinity chromatography on a glutathione S‐transferase fusion protein that… 
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References

SHOWING 1-10 OF 84 REFERENCES
Proteins Associated with α1‐Subunit‐Containing GABAA Receptors from Bovine Brain
TLDR
Peptide mass fingerprinting analysis and microsequencing of tryptic peptides indicated that at least three GTAPs have not been described until the present, and results of a biochemical characterization of these GABAA receptor‐tubulin complex‐associated proteins (GTAPs) are presented.
Domains involved in the specificity of G protein activation in phospholipase C‐coupled metabotropic glutamate receptors.
TLDR
It is reported here that both the C‐terminal end of the second intracellular loop and the segment located downstream of the seventh transmembrane domain are necessary for the specific activation of PLC by mGluR1c, indicating that whereas no amino acid sequence homology between mGLURs and the other G protein‐coupled receptors can be found, their G protein interacting domains have similar structural features.
The Metabotropic Glutamate Receptor mGluR4, but Not mGluR1α, Is Palmitoylated when Expressed in BHK Cells
TLDR
The palmitoylated, endogenously expressed G protein α‐subunit αq could be immunoprecipitated from [3H]palmitate‐labelled BHK cells expressing mGluR1α using a specific antipeptide antibody, but in the same cell lysates no detectable palmitate was found, suggesting that this mGLUR subtype, associated with stimulation of phospholipase C, is not palMIToylated.
Interaction between the C terminus of NMDA receptor subunits and multiple members of the PSD-95 family of membrane-associated guanylate kinases
  • M. Niethammer, E. Kim, M. Sheng
  • Biology, Chemistry
    The Journal of neuroscience : the official journal of the Society for Neuroscience
  • 1996
TLDR
Data suggest that PDZ domains can function as modules for protein-protein interactions and members of the PSD-95 family might serve to anchor NMDA receptors to the submembrane cytoskeleton and aid in the assembly of signal transduction complexes at postsynaptic sites.
Molecular cloning and the functional expression of two isoforms of human metabotropic glutamate receptor subtype 5.
TLDR
It is shown that the glutamate-evoked responses appear in Xenopus oocytes while expressing either of the two mGluR5 isoforms, which suggests that these two receptors from the human brain could activate phospholipase C and generate Ca(2+)-activated Cl- current.
Proteins associated with alpha 1-subunit-containing GABAA receptors from bovine brain.
TLDR
Peptide mass fingerprinting analysis and microsequencing of tryptic peptides indicated that at least three GTAPs have not been described until the present, and results of a biochemical characterization of these GABAA receptor-tubulin complex-associated proteins (GTAPs) are presented.
Rat Brain Glyceraldehyde‐3‐Phosphate Dehydrogenase Interacts with the Recombinant Cytoplasmic Domain of Alzheimer's β‐Amyloid Precursor Protein
TLDR
It is suggested that the interaction of the cytoplasmic domain of APP with GAPDH is unlikely to influence directly the rate of glycolysis but may serve another function.
GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors
TLDR
GRIP is a new member of the PDZ domain-containing protein family which has seven PDZ domains and no catalytic domain and appears to serve as an adapter protein that links AMPA receptors to other proteins and may be critical for the clustering of AMPA receptor at excitatory synapses in the brain.
Role of the Second and Third Intracellular Loops of Metabotropic Glutamate Receptors in Mediating Dual Signal Transduction Activation*
TLDR
Two residues are uncovered that are crucial for coupling to both pathways, since their substitution leads to receptor inactivation, and are introduced within the second and third intracellular loops of mGluR1α.
...
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