GluA3 AMPA receptors are integral to excitatory neurotransmission, assembled from core and auxiliary subunits. They have both fast Ca2+-permeable and Ca2+-impermeable roles. Recent cryo-EM structures reveal that GluA3's architecture includes closely coupled extracellular domain tiers, producing new interfaces crucial for signaling. Notably, interactions involving Arg163 in the NTD dimer affect receptor dynamics and trafficking. These specific design features influence GluA3's biogenesis and stability, shedding light on its involvement in neurological disorders and offering a framework for further investigation into this disease-associated receptor.
Cryoelectron microscopy reveals novel structures of the GluA3 homomer, highlighting unique interfaces that impact signaling and are relevant to human disease mutations.
GluA3 demonstrates dual functionality, acting as both a Ca2+-permeable receptor in sensory synapses and a Ca2+-impermeable receptor in cortical synapses, reflecting its molecular diversity.
Central to GluA3's architecture is a stacking interaction of Arg163 in the NTD dimer interface, which stabilizes a unique dimer conformation critical for receptor dynamics.
The binding interactions and conformational stability in GluA3 are essential for its trafficking and expression at synapses, providing insights into its role in excitatory neurotransmission.
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