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. 2009 Feb 24;106(11):4507–4512. doi: 10.1073/pnas.0900355106

Fig. 5.

Fig. 5.

Loss of ErbB2/B4 affects interactions between NMDAr and PSD-95. (A) Hippocampal neurons from WT and ErbB2/B4-CNSko mice transfected with eGFP (green) were stained at DIV21 with antibodies to PSD-95 (red) and NMDAr subunit NR1 (blue). Higher magnifications with red and blue channels are also shown separately in gray. (B) The density of PSD-95 and NR1 clusters was reduced in mutants. NR1 density (clusters/10 μm]: WT 6.92 ± 0.45, n = 465 clusters from 10 neurons; ErbB2/B4-CNSko 4.17 ± 0.43, n = 353 clusters from 11 neurons, ***P < 0.001; PSD-95 density (clusters/10 μm): WT 6.9 ± 0.52, n = 464 clusters from 10 neurons; ErbB2/B4-CNSko 4.19 ± 0.36, n = 347 clusters from 11 neurons, ***P < 0.001. (C) In ErbB2/B4-CNSko neurons the percentage of co-localization of NR1 and PSD-95 clusters was reduced (%): WT 23.25 ± 0.85, ErbB2/B4-CNSko 16.88 ± 1.17, ***P < 0.001). (D) Co-immunoprecipitation of NR1, NR2A or NR2B with PSD-95 revealed a 64.8 ± 8.1% (*P < 0.05), 34.5 ± 2.5% (**P < 0.01), and 30.2 ± 5.7% (**P < 0.01) decrease of protein interactions in mutants. Reverse co-immunoprecipitation of PSD-95 with NR1 also showed a reduction of 18.2 ± 1.7% (**P < 0.01). For each co-immunoprecipitation assay, the amount of immunoprecipitated protein revealed by immunoblotting is also presented. Negative controls for co-immunoprecipitation assays are shown in Fig. S7C. Scale bars, 10 μm.