Architecture of the heteromeric GluA1/2 AMPA receptor in complex with the auxiliary subunit TARP γ8

Author:

Herguedas Beatriz1ORCID,Watson Jake F.1ORCID,Ho Hinze1,Cais Ondrej1,García-Nafría Javier2ORCID,Greger Ingo H.1ORCID

Affiliation:

1. Neurobiology Division, Medical Research Council (MRC) Laboratory of Molecular Biology, Cambridge, UK.

2. Structural Studies Division, MRC Laboratory of Molecular Biology, Cambridge, UK.

Abstract

Regulating signals at synapses At excitatory synapses in the brain, tetrameric cation channels called AMPA-type glutamate receptors (AMPARs) play a key role in the cellular processes that underlie learning and memory. AMPARs are heterotetramers comprising various compositions of the subunits GluA1 to 4. Herguedas et al. used cryo–electron microscopy to determine the structure of the most prevalent form of AMPAR in the hippocampus, the GluA1/2 heteromer in complex with its regulatory subunit TARPγ8. The structure shows the architecture of the complex and provides insight into how conductance is controlled and modulated by auxiliary subunits. Science , this issue p. eaav9011

Funder

Medical Research Council

Heptares Therapeutics

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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