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The dynamic AMPA receptor extracellular region: a platform for synaptic protein interactions
Author(s) -
GarcíaNafría J.,
Herguedas B.,
Watson J. F.,
Greger I. H.
Publication year - 2016
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jp271844
Subject(s) - ampa receptor , neurotransmission , neuroscience , synaptic plasticity , chemistry , excitatory postsynaptic potential , biophysics , glutamate receptor , microbiology and biotechnology , receptor , biology , biochemistry
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 ∼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.