Over the last few years, first with the advent of yeast 2-hybrid technology and then with improved immunoprecipitation techniques and the development of proteomics, it has become clear that receptor proteins operate within a complex web of interactions with other proteins that goes far beyond well known phosphorylation and dephosphorylation cycles. Many interactions serve to modulate the transport, localisation and mobility of receptor molecules, while others affect their acute functioning. Many proteins have been found that interact directly with glutamate receptors (some with more than one subtype), while many more interact indirectly. This gives rise to vast and complex network of protein-protein interactions that can have a profound effect on synaptic function.
The table shows the major interacting proteins for each class of glutamate receptor while the links to following pages detail three structure and functions. These do not include the protein kinases and phosphatases that perform (de)phosphorylation on these proteins, as numerous such interaction sites exits on each receptor subunit/type.
