Error creating thumbnail: File missingSong and Huganir 2002. Use of yeast two-hybrid method to identify AMPA-receptor-interacting proteins was crucial for the rapid progress in this field and has helped to identify a large complex of such proteins. AMPA-receptor-associated protein complex. AMPA receptors are associated with a large protein network. The GluR2 subunit specifically binds to several proteins, including glutamatereceptor- interacting protein (GRIP) 1, GRIP2, protein interacting with C kinase (PICK1) and N-ethylmaleimide sensitive factor (NSF). GRIP1, GRIP2 and PICK1 in turn bind to other proteins, including GRIP-associated proteins (GRASPs), EphB receptor tyrosine kinases, ephrins, kinesin 5 (KIF5) and protein kinase Cα (PKCα). The GluR1 subunit binds to synapse-associated protein 97 (SAP97, also known as hDLG) and protein 4.1 (4.1 N). All four AMPA-receptor subunits bind to neuronal activity regulated pentraxin (NARP) and stargazin. Stargazin binds, in turn, to the synaptic scaffolding protein postsynaptic density 95 (PSD95). These associated proteins appear to play an important role in the membrane trafficking of the receptors by escorting the receptor from the cell body to the synapse. In addition, this large complex might regulate novel downstream signal transduction pathways that emanate from the AMPA receptor. Abbreviations: CC, coiled-coil domain; GK, guanylate kinase domain; PDZ, PSD95/Dlg/ZO1 domain; SH3, SRC homology 3 domain.
