Structural mobility tunes signalling of the GluA1 AMPA glutamate receptor.

ABSTRACT: AMPA glutamate receptors (AMPARs), the primary mediators of excitatory neurotransmission in the brain, are either GluA2 subunit-containing and thus Ca²⁺-impermeable, or GluA2-lacking and Ca²⁺-permeable¹. Despite their prominent expression throughout interneurons and glia, their role in long-term potentiation and their involvement in a range of neuropathologies², structural information for GluA2-lacking receptors is currently absent. Here we determine and characterize cryo-electron microscopy structures of the GluA1 homotetramer, fully occupied with TARPγ3 auxiliary subunits (GluA1/γ3). The gating core of both resting and open-state GluA1/γ3 closely resembles GluA2-containing receptors. However, the sequence-diverse N-terminal domains (NTDs) give

SUBMITTER: Zhang D 

PROVIDER: S-EPMC10533411 | biostudies-literature | 2023 Sep

REPOSITORIES: biostudies-literature