Eileen R. Mulvihill

TL;DR: Electron microscopic immunometal detection of mGluR1 alpha showed a preferential localization at the periphery of the extensive postsynaptic densities of type 1 synapses in both the cerebellum and the hippocampus.

TL;DR: Sensitive sequence analysis techniques indicate that the metabotropic receptor extracellular domain is similar to bacterial periplasmic amino acid binding proteins, and a structural model built using the observed similarity predicts a ligand-binding site, and mutants with conservative amino acid substitutions at this site are shown to have reduced ligand affinity.

TL;DR: A complementary DNA encoding a G protein-coupled glutamate receptor from rat brain, GluGR, was cloned by functional expression in Xenopus oocytes, suggesting that it may be a member of a new subfamily.

TL;DR: It is suggested that the spatial segregation of ionotropic and metabotropic glutamate receptors permits the differential activation of these receptors according to the amount of glutamate released presynaptically, whereas the different densities of the ionotropic receptor at distinct synapses could allow the same amount of glutamate to evoke fast responses of different magnitude.

TL;DR: It is demonstrated that mGluR4 receptors arc negatively coupled to the cAMP cascade, and it is suggested that the mGLUR4 receptor may be the previously described presynaptic L-AP4 receptor.