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Cell-surface protein-protein interaction analysis with time-resolved FRET and snap-tag technologies: application to GPCR oligomerization
TLDR
A methodology combining time-resolved fluorescence resonance energy transfer (FRET) with snap-tag technology to quantitatively analyze protein-protein interactions at the surface of living cells, in a high throughput–compatible format is described.
CPCCOEt, a noncompetitive metabotropic glutamate receptor 1 antagonist, inhibits receptor signaling without affecting glutamate binding.
TLDR
It is proposed that the interaction of CPCCOEt with Thr815 and Ala818 of mGluR1 disrupts receptor activation by inhibiting an intramolecular interaction between the agonist-bound extracellular domain and the transmembrane domain.
Activation mechanism of the heterodimeric GABA(B) receptor.
The Non-competitive Antagonists 2-Methyl-6-(phenylethynyl)pyridine and 7-Hydroxyiminocyclopropan[b]chromen-1a-carboxylic Acid Ethyl Ester Interact with Overlapping Binding Pockets in the
TLDR
Results indicate that MPEP and CPCCOEt bind to overlapping binding pockets in the TM region of group I mGluRs but interact with different non-conserved residues.
Agonist-independent activation of metabotropic glutamate receptors by the intracellular protein Homer
TLDR
In neurons, the constitutive activity of these receptors is controlled by Homer proteins, which bind directly to the receptors' carboxy-terminal intracellular domains, which show that these glutamate GPCRs can be directly activated by intraceocytes as well as by agonists.
Allosteric interactions between GB1 and GB2 subunits are required for optimal GABAB receptor function
TLDR
The data indicate that multiple allosteric interactions between the two subunits are required for wild‐type functioning of the GABAB receptor and highlight further the importance of the dimerization process in GPCR activation.
C-Terminal Interaction Is Essential for Surface Trafficking But Not for Heteromeric Assembly of GABAB Receptors
TLDR
This work investigated the mechanism underlying GABAB(1) trafficking to the cell surface and identified a signal, RSRR, proximal to the coiled-coil domain of GABAB (1) that when deleted or mutagenized allows for surface delivery in the absence of GABA B(2).
Heptahelical domain of metabotropic glutamate receptor 5 behaves like rhodopsin-like receptors
  • C. Goudet, F. Gaven, J. Pin
  • Biology, Chemistry
    Proceedings of the National Academy of Sciences…
  • 22 December 2003
TLDR
It is shown that the HD of metabotropic glutamate receptor 5 (mGlu5) displays the same agonist-independent constitutive activity as the wild-type receptor, and illustrates that, like rhodopsin-like receptors, theHD of mGluRs can constitutively couple to G proteins and be negatively and positively regulated by ligands.
Changes in the carboxyl-terminal domain of metabotropic glutamate receptor 1 by alternative splicing generate receptors with differing agonist-independent activity.
TLDR
Surprisingly none of the known competitive antagonists of mGluR1 inhibited the basal PLC activity, indicating that none of these molecules act as inverse agonists, and the results indicate that the long carboxyl-terminal domain confers a small agonist-independent activity to mGLUR1.
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