Introduction of single photoswitchable unnatural amino acid into a neuronal receptor provides reversible, rapid and robust control of its activity by light, representing an important contribution to the fast expanding field of optopharmacology.
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.
Glutamate receptor auxiliary proteins exert their effects on receptor gating through two divergent extracellular loops, explaining subunit specificity and allowing the construction of null versions that form complexes normally but do not modify receptor gating.
Electrically active axons in white matter stimulate their own myelination by releasing glutamate, which signals through AMPA-type glutamate receptors on nearby oligodendrocyte precursors and newly-differentiating oligodendrocytes, enhancing their survival and hence their ability to myelinate.
Male and female mice differ in basal cerebellar physiology, including the magnitude of synaptic excitation by metabotropic glutamate receptors, kinetics of synaptic inhibition, intrinsic properties, and responses to autism-linked mutations.
In mouse models of Huntington's disease, the subthalamic nucleus, which suppresses movements, also exhibits impaired glutamate homeostasis, NMDA receptor-dependent mitochondrial oxidant stress, firing disruption, and 30% neuronal loss.
Members of kainate and AMPA families of glutamate receptors exhibit large differences in affinity for homo- and hetero-dimerziation of their amino terminal domains, which may control gating characteristics and ion selectivity of receptor subtypes with different subunit composition.