The article discusses the essential role of AMPA-type ionotropic glutamate receptors (AMPARs) in synaptic transmission, plasticity, and memory. While significant research has focused on various types of AMPARs, the article presents new findings on native calcium permeable AMPARs (CP-AMPARs) through cryo-electron microscopy. The study identifies GluA1 and GluA4 as the key subunits in CP-AMPARs and highlights the role of Noelin 1 in stabilizing receptor structures and enhancing functionality. This discovery offers insights into receptor clustering and modulation, impacting synaptic transmission dynamics.
Our results indicate that the predominant assembly consists of GluA1 and GluA4 subunits, with the GluA4 subunit occupying the B and D positions.
Noe 1 stabilizes the amino-terminal domain (ATD) layer without affecting receptor gating properties, contributing to AMPAR function by forming dimeric-AMPAR assemblies.
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