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High-resolution proteomics unravel architecture and molecular diversity of native AMPA receptor complexes.

Authors: Schwenk, J  Harmel, N  Brechet, A  Zolles, G  Berkefeld, H  Muller, CS  Bildl, W  Baehrens, D  Huber, B  Kulik, A  Klocker, N  Schulte, U  Fakler, B 
Citation: Schwenk J, etal., Neuron. 2012 May 24;74(4):621-33. doi: 10.1016/j.neuron.2012.03.034.
Pubmed: (View Article at PubMed) PMID:22632720
DOI: Full-text: DOI:10.1016/j.neuron.2012.03.034

AMPA-type glutamate receptors (AMPARs) are responsible for a variety of processes in the mammalian brain including fast excitatory neurotransmission, postsynaptic plasticity, or synapse development. Here, with comprehensive and quantitative proteomic analyses, we demonstrate that native AMPARs are macromolecular complexes with a large molecular diversity. This diversity results from coassembly of the known AMPAR subunits, pore-forming GluA and three types of auxiliary proteins, with 21 additional constituents, mostly secreted proteins or transmembrane proteins of different classes. Their integration at distinct abundance and stability establishes the heteromultimeric architecture of native AMPAR complexes: a defined core with a variable periphery resulting in an apparent molecular mass between 0.6 and 1 MDa. The additional constituents change the gating properties of AMPARs and provide links to the protein dynamics fundamental for the complex role of AMPARs in formation and operation of glutamatergic synapses.

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RGD ID: 8553757
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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RGD is funded by grant HL64541 from the National Heart, Lung, and Blood Institute on behalf of the NIH.