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GluA2 (GRIA2 or GluR2) is a subunit of the AMPA-type ionotropic glutamate receptor, mediating fast excitatory neurotransmission in the CNS. GluA2's presence and RNA editing status (Q/R site) determine key properties like Ca²⁺ permeability and inward rectification. It also regulates AMPAR trafficking, a critical process for synaptic plasticity. Interactions involving the extracellular domain of GluA2 with N-cadherin regulate metabotropic glutamate receptor-dependent long-term depression. The structure of GluA2 has been solved, informing drug design targeting specific functional states or isoform compositions.
Agonist binding leading to ion channel opening and neuronal excitation; modulation of receptor activity via allosteric binding sites.
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