A novel form of hippocampal synaptic plasticity is expressed by a change in channel function of GluA3-containing AMPA-receptors.

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.

Small probes show that most AMPA receptors are constrained near or in the synapses.

The positioning of AMPA-type glutamate receptors at synapses – a requirement for effective neurotransmission and synaptic plasticity – is orchestrated by their extracellular, N-terminal domain.

There are at least two separate pathways for AMPA receptor recycling, which are regulated by synaptic activity.

Neurons in the hypothalamus that promote satiety manifest plasticity of their response to the excitatory transmitter, glutamate, by re-organizing the composition of a specific glutamare receptor.

Three AMPAR interacting proteins – namely CKAMP39, CKAMP52 and CKAMP59 – together with the previously characterized CKAMP44, constitute a new family of auxiliary subunits that are distinct from other families of AMPAR interacting proteins.

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.

The auxiliary protein Stargazin limits the conformational dynamics of AMPA-type glutamate receptors in cell membranes, as revealed by 'molecular rulers' deployed on the seconds to milliseconds timescale.