Fig. 3 Active p38γ dissociates PSD-95/tau/Fyn/NR complexes.

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Fig. 3 Active p38γ dissociates PSD-95/tau/Fyn/NR complexes. Active p38γ dissociates PSD-95/tau/Fyn/NR complexes. (A) Immunoprecipitation (IP) analysis. More PSD-95/tau/Fyn complexes were immunoprecipitated from the brains of Alz17.p38γ−/− than Alz17.p38γ+/+ animals, despite comparable total protein levels. Detection of glyceraldehyde-3-phosphate dehydrogenase (GAPDH) confirmed equal loading (n = 6). Numbers at right indicate molecular weight. a.i., arbitrary index. (B) p38γ (WT) and p38γCA (CA) failed to disrupt PSD-95/tau/Fyn complexes in the presence of the p38 inhibitor (n = 6). p38 inhibition reduces phosphorylated active p38 levels (p-p38). (C) More tau, Fyn, and NMDA receptor subunits 1 (NR1) and 2B (NR2B) were immunoprecipitated with PSD-95 from p38γ−/− versus p38γ+/+ brains. This result was further enhanced in APP23.p38γ−/− mice compared with APP23.p38γ+/+ animals, without changes to total protein levels (n = 6 to 8). (D) Virtually no PSD-95/tau/Fyn complexes were immunoprecipitated from the brains of p38γCA-expressing mice (n = 6). For all panels: Representative blots are shown. Quantification of IP bands relative to PSD-95 IP. ***P < 0.001; **P < 0.01; *P < 0.05. Error bars indicate SEM. Arne Ittner et al. Science 2016;354:904-908 Copyright © 2016, American Association for the Advancement of Science