title: Assembly of AMPA receptors: mechanisms and regulation.
abstract: 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.
authors.affiliation: Graduate Program in Neuroscience, Stony Brook University, Stony Brook, NY, USA; Center for Nervous System Disorders, Stony Brook University, Stony Brook, NY, USA; Department of Neurobiology and Behaviour, Stony Brook University, Stony Brook, NY, USA.
authors.forename: Quan
authors.initials: Q
authors.lastname: Gan
authors.forename: Catherine L
authors.initials: CL
authors.lastname: Salussolia
authors.forename: Lonnie P
authors.initials: LP
authors.lastname: Wollmuth
mesh_terms: D006801:Humans; D008958:Models, Molecular; D055503:Protein Multimerization; D017434:Protein Structure, Tertiary; D018091:Receptors, AMPA / Q000737:chemistry / Q000378:metabolism
chemical_list: D018091:Receptors, AMPA