Single molecule subunit counting, FRET and electrophysiology experiments reveal that metabotropic glutamate receptor subunits interact and rearrange at the level of the transmembrane domains in response to allosteric modulators.

During parallel fibre activity in vivo, postsynaptic mGluR1 receptors in molecular layer interneurons of the cerebellar cortex are engaged in a frequency-dependent manner and in concert with inotropic glutamate receptors.

Homo- and heterodimeric group II metabotropic glutamate receptors show diverse modes of interaction between transmembrane domains that control their distinct assembly and activation properties.

Group III metabotropic glutamate receptor inhibition facilitates synaptic plasticity in the plasticity-resistant synapses of hippocampal area CA2, a brain region critical for social memory.

Innovative approaches were used to identify the specific pharmacological properties of heterodimeric metabotropic glutamate receptors composed of mGlu2 and mGlu4 subunits, and reveal their existence in a neuronal cell line and in perforant path terminals.

Localized drug photoactivation provides light-mediated analgesia in behaving mice.

Estrogen increases hypothalamic arcuate kisspeptin neuronal excitability and glutamate release to coordinate autonomic functions for maximizing reproductive success.

Dopamine neurons make novel glutamatergic connections to striatal cholinergic interneurons in the lateral dorsal striatum that are mediated by metabotropic glutamate receptors coupled to TrpC channels.

A combination of single-molecule and in vivo FRET showed how drugs affect conformation of mGluR2 at different domains.

In mGlu heterodimers, an oriented asymmetrical activation revealed complex allosteric interaction between subunits.