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Assembly of AMPA receptors: mechanisms and regulation
Author(s) -
Gan Quan,
Salussolia Catherine L.,
Wollmuth Lonnie P.
Publication year - 2014
Publication title -
the journal of physiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.802
H-Index - 240
eISSN - 1469-7793
pISSN - 0022-3751
DOI - 10.1113/jphysiol.2014.273755
Subject(s) - ampa receptor , glutamatergic , silent synapse , microbiology and biotechnology , neurotransmission , neuroscience , receptor , chemistry , protein subunit , transmembrane domain , transmembrane protein , biology , glutamate receptor , biophysics , biochemistry , gene
AMPA receptors (AMPARs) play a critical role in excitatory glutamatergic neurotransmission. The number and subunit composition of AMPARs at synapses determines the dynamics of fast glutamatergic signalling. Functional AMPARs on the cell surface are tetramers. Thus tetrameric assembly of AMPARs represents a promising target for modulating AMPAR‐mediated signalling in health and disease. Multiple structural domains within the receptor influence AMPAR assembly. In a proposed model for AMPAR assembly, the amino‐terminal domain underlies the formation of a dimer pool. The transmembrane domain facilitates the formation and enhances the stability of the tetramer. The ligand‐binding domain influences assembly through a process referred to as ‘domain swapping’. We propose that this core AMPAR assembly process could be regulated by neuronal signals and speculate on possible mechanisms for such regulation.