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Functional proteomics identify cornichon proteins as auxiliary subunits of AMPA receptors.

Authors: Schwenk, J  Harmel, N  Zolles, G  Bildl, W  Kulik, A  Heimrich, B  Chisaka, O  Jonas, P  Schulte, U  Fakler, B  Klocker, N 
Citation: Schwenk J, etal., Science. 2009 Mar 6;323(5919):1313-9. doi: 10.1126/science.1167852.
Pubmed: (View Article at PubMed) PMID:19265014
DOI: Full-text: DOI:10.1126/science.1167852

Glutamate receptors of the AMPA-subtype (AMPARs), together with the transmembrane AMPAR regulatory proteins (TARPs), mediate fast excitatory synaptic transmission in the mammalian brain. Here, we show by proteomic analysis that the majority of AMPARs in the rat brain are coassembled with two members of the cornichon family of transmembrane proteins, rather than with the TARPs. Coassembly with cornichon homologs 2 and 3 affects AMPARs in two ways: Cornichons increase surface expression of AMPARs, and they alter channel gating by markedly slowing deactivation and desensitization kinetics. These results demonstrate that cornichons are intrinsic auxiliary subunits of native AMPARs and provide previously unknown molecular determinants for glutamatergic neurotransmission in the central nervous system.

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RGD Object Information
RGD ID: 8554136
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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