Abstract:
:AMPA receptors are thought to be a tetrameric assembly of the subunits GluR1-4. We have examined whether two coexpressed subunits (GluR1/2) combine at random to form channels, or preferentially assemble with a specific stoichiometry and spatial configuration. The subunits carried markers controlling ion permeation and desensitization, and these properties were monitored as a function of relative expression level and subunit composition. Homomeric receptors assembled stochastically while heteromeric receptors preferentially formed with a stoichiometry of two GluR1 and two GluR2 subunits, and with identical subunits positioned on opposite sides of the channel pore. This structure will predominate if GluR1 binds to GluR2 more rapidly during receptor assembly than other subunit combinations. The practical outcome of selective heteromeric assembly is a more homogenous receptor population in vivo.
journal_name
Neuronjournal_title
Neuronauthors
Mansour M,Nagarajan N,Nehring RB,Clements JD,Rosenmund Cdoi
10.1016/s0896-6273(01)00520-7subject
Has Abstractpub_date
2001-12-06 00:00:00pages
841-53issue
5eissn
0896-6273issn
1097-4199pii
S0896-6273(01)00520-7journal_volume
32pub_type
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