THE AMPA RECEPTOR GLUR2 C-TERMINUS CAN MEDIATE A REVERSIBLE, ATP-DEPENDENT INTERACTION WITH NSF AND ALPHA-SNAPS AND BETA-SNAPS

In this study, we demonstrate specific interaction of the GluR2 ha-ami no-3-hydroxy-5-methyl-4-isoxazole-propionate (AMPA) receptor subunit c -terminal peptide with an ATPase N-ethylmaleimide-sensitive fusion pro tein (NSF) and alpha- and beta-soluble NSF attachment proteins (SNAPs) , as well as dendritic colocalization of these proteins. The assembly of the GluR2-NSF-SNAP complex is ATP hydrolysis reversible and resembl es the binding of NSF and SNAP with the SNAP receptor (SNARE) membrane fusion apparatus. We provide evidence that the molar ratio of NSF to SNAP in the GluR2-NSF-SNAP complex is similar to that of the t-SNARE s yntaxin-NSF-SNAP complex. NSF is known to disassemble the SNARE protei n complex in a chaperone-like interaction driven by ATP hydrolysis. We propose a model in which NSF functions as a chaperone in the molecula r processing of the AMPA receptor.