... blots of lysates of Y394F tau(Fig. 2A). The absence of this larger species could indi-cate that phosphorylation of tau by Fyn is reducedand therefore, in addition to phosphorylation by c-Abl[25], ... interaction is regulated by serine ⁄ threonine phosphorylation of tau [20,21]. To determine whether the tyrosine phosphorylation status of tau also affects the binding of tau to Fyn-SH3, CHO cells ... predominantly by c-Abl. However,impaired phosphorylation of Tyr394 did not appearto influence the binding of tau to Fyn-SH2, as therewas no significant difference in the amount of Y394Fthat...