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• W2467790803 abstract "The cryo-electron microscopy structure of the homomeric GluA2 AMPA receptor in the presence of TARP γ2 subunits is reported, which reveals that TARPs are arranged around the ion channel domain and underneath the ligand-binding domains, poised to modulate receptor activity. The bulk of the fast excitatory neurotransmission taking place in the mammalian central nervous system involves AMPA-sensitive ionotropic glutamate receptors. AMPA receptors are composed of heterotetrameric receptor assemblies associated with auxiliary subunits, the most common of which are transmembrane AMPA-receptor regulatory proteins (TARPs). Eric Gouaux and colleagues report the cryo-electron microscopy structure of the homomeric GluA2 AMPA receptor in the presence of TARP γ2 subunits. The structure reveals that TARPs are arranged with four-fold symmetry around the ion channel domain, making extensive interactions with the M1, M2 and M4 transmembrane helices. The authors propose a mechanism by which TARP γ2 modulates the gating of the AMPA receptor. Fast excitatory neurotransmission in the mammalian central nervous system is largely carried out by AMPA-sensitive ionotropic glutamate receptors1. Localized within the postsynaptic density of glutamatergic spines, AMPA receptors are composed of heterotetrameric receptor assemblies associated with auxiliary subunits, the most common of which are transmembrane AMPA receptor regulatory proteins (TARPs). The association of TARPs with AMPA receptors modulates receptor trafficking and the kinetics of receptor gating and pharmacology2. Here we report the cryo-electron microscopy (cryo-EM) structure of the homomeric rat GluA2 AMPA receptor saturated with TARP γ2 subunits, which shows how the TARPs are arranged with four-fold symmetry around the ion channel domain and make extensive interactions with the M1, M2 and M4 transmembrane helices. Poised like partially opened ‘hands’ underneath the two-fold symmetric ligand-binding domain (LBD) ‘clamshells’, one pair of TARPs is juxtaposed near the LBD dimer interface, whereas the other pair is near the LBD dimer–dimer interface. The extracellular ‘domains’ of TARP are positioned to not only modulate LBD clamshell closure, but also affect conformational rearrangements of the LBD layer associated with receptor activation and desensitization, while the TARP transmembrane domains buttress the ion channel pore." @default.
• W2467790803 created "2016-07-22" @default.
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• W2467790803 date "2016-07-01" @default.
• W2467790803 modified "2023-10-04" @default.
• W2467790803 title "Architecture of fully occupied GluA2 AMPA receptor–TARP complex elucidated by cryo-EM" @default.
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• W2467790803 doi "https://doi.org/10.1038/nature18961" @default.
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