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• W1988936224 endingPage "841" @default.
• W1988936224 startingPage "832" @default.
• W1988936224 abstract "Metabotropic glutamate receptor 1 (mGlu1) functions as a homodimer and activates not only the Gq but also the Gi/o and Gs pathways. Because of the dimeric configuration, different pathways could be activated either through the glutamate-bound subunit (cis-activation) and/or the other one (trans-activation). We here examined whether the intra-molecular activation mechanisms in the mGlu1 differ depending on the type of coupling G proteins, using various combinations of mGlu1 constructs that lack glutamate binding and/or G-protein coupling. The cis- or trans-activation alone was confirmed to trigger the Gq-coupled intracellular Ca(2+) transient. In contrast, the Gi/o-coupled G protein-dependent inward rectifying potassium (GIRK) channels were not activated either through the cis- or trans-activation alone. When one subunit of dimeric mGlu1 lacked the G-protein coupling, a significant decrease in the glutamate-induced GIRK current density was also observed. As the G protein-coupling-deficient subunit did not decrease the cell surface expression of mGlu1 and the Gq-coupled Ca(2+) transient, it was suggested that the coupling deficiency in one subunit of mGlu1 attenuates the Gi/o but not Gq coupling. In conclusion, multiple G-protein signaling was differentially activated by different intra-molecular activation mechanisms of the dimeric mGlu1." @default.
• W1988936224 created "2016-06-24" @default.
• W1988936224 creator A5025811508 @default.
• W1988936224 creator A5088049227 @default.
• W1988936224 date "2011-09-01" @default.
• W1988936224 modified "2023-09-24" @default.
• W1988936224 title "The intra-molecular activation mechanisms of the dimeric metabotropic glutamate receptor 1 differ depending on the type of G proteins" @default.
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• W1988936224 doi "https://doi.org/10.1016/j.neuropharm.2011.05.031" @default.
• W1988936224 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/21672544" @default.
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