An unbiased proteomic approach identifies a new regulator of AMPA receptor trafficking providing additional insight into synaptic transmission and plasticity.

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.

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.

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.

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

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

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.

Biochemistry, videomicroscopy, and immunocytochemistry reveal differential roles of GluA1/4.1N and GluA1/SAP97 interactions on GluA1 intracellular transport and exocytosis in basal transmission and during cLTP in cultured hippocampal neurons.

Intracellular NASPM, unlike the widely used spermine, fully blocks outward currents through calcium-permeable AMPA-type glutamate receptors, enabling an improved functional readout for this physiologically important receptor subtype in neurons.