Architecture, dynamics and biogenesis of GluA3 AMPA glutamate receptors.

ABSTRACT: AMPA-type glutamate receptors (AMPARs) mediate the majority of excitatory neurotransmission in the brain¹. Assembled from combinations of four core subunits, GluA1-4 and around 20 auxiliary subunits, their molecular diversity tunes information transfer and storage in a brain-circuit-specific manner. GluA3, a subtype strongly associated with disease², functions as both a fast-transmitting Ca²⁺-permeable AMPAR at sensory synapses³, and as a Ca²⁺-impermeable receptor at cortical synapses^4,5. Here we present cryo-electron microscopy structures of the Ca²⁺-permeable GluA3 homomer, which substantially diverges from other AMPARs. The GluA3 extracellular domain tiers (N-terminal domain (NTD) and ligand-binding domain (LBD

SUBMITTER: Pokharna A 

PROVIDER: S-EPMC12422969 | biostudies-literature | 2025 Sep

REPOSITORIES: biostudies-literature