Fig. 1: A GluA2-specific NTD interface.
a, Left: schematic of an AMPAR tetramer, depicting the three domain layers and the inner BD subunits (light red), forming an interface between the GluA2 NTDs (boxed). Right: schematic of GluA2-containing AMPAR heteromers, where GluA2 localizes to the BD positions. b, Zoomed-in view of the GluA2 BD NTD interface (boxed); the vertical arrow denotes the two-fold symmetry axis. c, Top view of the further zoomed-in view of the GluA2 BD interface, showing the major interacting residues, including H208 and the cation–π interaction between R172 and F231. d, Sequence alignment of mouse AMPAR paralogs, showing divergence around the central histidine (blue) and the phenylalanine (brown) at the edges of the interface. e, Recovery from desensitization time constants for various mutants in GluA2 BD NTD interface, recorded at pH 7.4. Number of patches (GluA2 wt, n = 47; R172A, n = 10; I203A, n = 25; H208A, n = 31; F231A, n = 14; F231R, n = 14; H208A;F231A, n = 5). Bars show the mean and error bars denote the s.d. The effect of the substitution was determined by a one-way analysis of variance (ANOVA), F(6,139) = 26.36, followed by Dunnett’s multiple-comparisons test. ****P < 0.0001.
