Research Article

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

See allHide authors and affiliations

Science  26 Apr 2019:
Vol. 364, Issue 6438, eaav9011
DOI: 10.1126/science.aav9011

You are currently viewing the editor's summary.

View Full Text

Log in to view the full text

Log in through your institution

Log in through your institution

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