Functional assembly of AMPA and kainate receptors is mediated by several discrete protein-protein interactions.

摘要: Functional heterogeneity of ionotropic glutamate receptors arises not only from the existence many subunits and isoforms, but also combinatorial assembly creating channels with distinct properties. This heteromerization is subtype restricted thought to be determined exclusively by proximal extracellular N-terminal domain subunits. However, using functional assays for heteromer formation, we show that, besides domain, membrane sector C-terminal part S2 are critical determinants formation channels. Our results compatible a model where mediates initial subunit associations into dimers, whereas full tetramer, compatibility other regions required.