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The mGluR proteins (metabotropic glutamate receptors) are members of the G protein-coupled receptor family and are functionally and pharmacologically distinct from the GluR proteins (ionotropic glutamate receptors). The eight currently known mGluR proteins are mediated by two G proteins with opposing regulation of adenylate cyclase pathways. The activities of mGluR1 and mGluR5 are mediated by a G protein that activates a phosphatidylinositolcalcium second messenger system and generates a calcium-activated chloride current. The remainder of the eight subtypes of mGluR have an activity mediated by a G protein that inhibits adenylate cyclase activity. GLuR-8 is a group III metabotropic glutamate receptor. In response to glutamate stimulation, GLuR-8 activates GTP-binding proteins that modulate second-messenger cascades. Alternative splicing of this integral membrane protein produces three isoforms: a, b and c. Human GLuR-8 maps to q31.3-q32.1 of chromosome 7.
