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
Neuronjournal_title
Neuronauthors
Greger IH,Khatri L,Kong X,Ziff EBdoi
10.1016/s0896-6273(03)00668-8subject
Has Abstractpub_date
2003-11-13 00:00:00pages
763-74issue
4eissn
0896-6273issn
1097-4199pii
S0896627303006688journal_volume
40pub_type
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