AMPA receptor tetramerization is mediated by Q/R editing.

Abstract:

:AMPA-type glutamate receptors (AMPARs) play a major role in excitatory synaptic transmission and plasticity. Channel properties are largely dictated by their composition of the four subunits, GluR1-4 (or A-D). Here we show that AMPAR assembly and subunit stoichiometry are determined by RNA editing in the pore loop. We demonstrate that editing at the GluR2 Q/R site regulates AMPAR assembly at the step of tetramerization. Specifically, edited R subunits are largely unassembled and ER retained, whereas unedited Q subunits readily tetramerize and traffic to synapses. This assembly mechanism restricts the number of the functionally critical R subunits in AMPAR tetramers. Therefore, a single amino acid residue affects channel composition and, in turn, controls ion conduction through the majority of AMPARs in the brain.

journal_name

Neuron

journal_title

Neuron

authors

Greger IH,Khatri L,Kong X,Ziff EB

doi

10.1016/s0896-6273(03)00668-8

subject

Has Abstract

pub_date

2003-11-13 00:00:00

pages

763-74

issue

4

eissn

0896-6273

issn

1097-4199

pii

S0896627303006688

journal_volume

40

pub_type

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