Nerve cells (neurons) communicate (via neurotransmitters) at specialized cell junctions called synapses. During synaptic transmission, neurotransmitter released from the presynaptic neuron activates receptors at the postsynaptic neuron, thereby converting a chemical signal (neurotransmitter) into a rapid electrical response. The major transmitter in the mammalian brain is glutamate, which acts on various types of receptors. AMPA-type glutamate receptors (AMPARs) are the fastest transmitter-gated receptors in the brain, permitting precise information transfer. AMPARs are also essential for the expression of synaptic plasticity, a process underlying learning and information storage in the brain. Malfunction of these receptors underlies various neurological disorders. AMPAR signalling is diverse which is largely due to the existence of different AMPAR complexes, which assemble in various combinations, in a poorly understood process. This early event in receptor ontogeny is central as it ultimately determines the efficacy and plasticity of glutamatergic signal transmission. AMPAR action occurs on the millisecond time scale, and accurate signalling requires the receptor to be located precisely opposite presynaptic transmitter release sites. Our work showed that an extracellular AMPAR segment, the N-terminal domain, is essential for receptor positioning most likely by interacting with to-be-identified synaptic cleft proteins. Since the NTD is highly sequence-diverse between AMPAR subunits it will mediate subtype-selective ‘synaptic anchorage’ which provides a mechanism to fine-tune signal transmission. The aim of our research is to shed light on the assembly mechanism, to characterise functionally diverse AMPAR complexes structurally allowing precise intervention, and to follow their fate during synaptic potentiation using electrophysiology and imaging approaches. We anticipate that this combined approach will permit unprecedented insight into the process of information storage at synapses in the brain.