Abstract:
: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.
journal_name
Neuronjournal_title
Neuronauthors
Schwenk J,Harmel N,Brechet A,Zolles G,Berkefeld H,Müller CS,Bildl W,Baehrens D,Hüber B,Kulik A,Klöcker N,Schulte U,Fakler Bdoi
10.1016/j.neuron.2012.03.034subject
Has Abstractpub_date
2012-05-24 00:00:00pages
621-33issue
4eissn
0896-6273issn
1097-4199pii
S0896-6273(12)00345-5journal_volume
74pub_type
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