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. Author manuscript; available in PMC: 2013 Apr 1.
Published in final edited form as: Neurobiol Aging. 2011 Jul 27;33(4):826.e15–826.e30. doi: 10.1016/j.neurobiolaging.2011.06.006

Fig. 5.

Fig. 5

Disease-associated tau modifications impair phosphorylation at Y18. (A) WT tau was rapidly phosphorylated at Y18 by fyn kinase. In contrast, fyn-mediated phosphorylation of Y18 in AT8 tau and Δ144–273 tau was reduced. Antibodies used were Tau7 for total tau and 9G3 for pY18 tau. (B) Analysis of pY18 tau levels by ELISA demonstrates that while the maximal level of phosphorylation was similar, the rate of Y18 phosphorylation in AT8 tau was significantly reduced compared to WT tau (two-way repeated measure ANOVA; * p<0.05 compared to WT tau). Both the rate and maximal level of phosphorylation at Y18 in Δ144–273 tau was dramatically reduced compared to WT tau and AT8 tau (# p<0.05 compared to WT and AT8 tau).