期刊
JOURNAL OF PHYSIOLOGY-LONDON
卷 594, 期 19, 页码 5449-5458出版社
WILEY
DOI: 10.1113/JP271844
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资金
- Medical Research Council [MC_U105174197]
- MRC [MC_U105174197] Funding Source: UKRI
- Medical Research Council [1570848, MC_U105174197] Funding Source: researchfish
AMPA receptors (AMPARs) are glutamate-gated cation channels that mediate fast excitatory neurotransmission and synaptic plasticity. Structures of GluA2 homotetramers in distinct functional states, together with simulations, emphasise the loose architecture of the AMPAR extracellular region (ECR). The ECR encompasses approximate to 80% of the receptor, and consists of the membrane-distal N-terminal domain (NTD) and ligand-binding domain (LBD), which is fused to the ion channel domain. Minimal contacts within and between layers, together with flexible peptide linkers connecting these three domains give rise to an organisation capable of dynamic rearrangements. This building plan is uniquely suited to engage interaction partners in the crowded environment of synapses, permitting the formation of new binding sites and the loss of existing ones. ECR motions are thereby expected to impact signalling as well as synaptic anchorage and may thereby influence AMPAR clustering during synaptic plasticity.
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