Journal
NEURON
Volume 74, Issue 4, Pages 621-633Publisher
CELL PRESS
DOI: 10.1016/j.neuron.2012.03.034
Keywords
-
Categories
Funding
- Deutsche Forschungsgemeinschaft [SFB 746/TP16, SFB780/A3, SFB780/A2]
- Medical Research Council [G9817803B] Funding Source: researchfish
Ask authors/readers for more resources
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 AM PAR 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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available