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Divalent cations modulate the activity of metabotropic glutamate receptors

✍ Scribed by Anna Francesconi; Robert M. Duvoisin

Publisher
John Wiley and Sons
Year
2004
Tongue
English
Weight
259 KB
Volume
75
Category
Article
ISSN
0360-4012

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✦ Synopsis

Abstract

Metabotropic glutamate receptors (mGluRs) and calcium receptors (CaR) are closely related G protein‐coupled receptors (GPCRs). The similar structural and functional properties of mGluRs and CaRs include conserved amino acid residues involved in glutamate binding in mGluRs and Ca^2+^ binding in the CaR. Furthermore, recent findings have demonstrated that mGluRs can respond to high extracellular Ca^2+^ (Ca) whereas CaR activity is potentiated by L‐amino acids. We show that both mGluR1 and mGluR2 are activated by Ca in the absence of glutamate in the extracellular media. This activation by Ca is antagonized by Mg. Unlike the CaR, in which the intracellular carboxyl tail has been reported to be involved in Ca‐dependent activity, the carboxyl tail of mGluRs does not seem to play a role in mediating Ca actions. On the other hand, we find that preservation of disulfide bonds in the N‐terminal extracellular domain of mGluRs is essential for stimulation by Ca as well as glutamate. Because the mGluR1 EC~50~ for Ca is within the physiologic range of Ca^2+^ in the synaptic cleft, mGluR function is likely regulated by changes in divalent cations caused by synaptic activity under normal or pathologic conditions. © 2003 Wiley‐Liss, Inc.

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