The Homologous Carboxyl-Terminal Domains of Microtubule-Associated Protein 2 and TAU Induce Neuronal Dysfunction and Have Differential Fates in the Evolution of Neurofibrillary Tangles
Figure 4
Biochemical characterizations of MAP2c and Tau expressed in transgenic C. elegans.
(A) Both MAP2c and Tau were highly phosphorylated in worm neurons. MAP2c and Tau (0N4R) were purified from the corresponding transgenic worms (MAP2c from tmIs849; 0N4R from tmIs390). Purified proteins were treated with or without phosphatase and subjected to western blotting using the HT7 (anti-human Tau monoclonal) and HM2 (anti-MAP2 monoclonal). (B) MAP2c and Tau did not bind to microtubules. The microtubules prepared were stabilized with taxol and GTP, and fractionated into the pellet (P) and supernatant (S). Both MAP2 and Tau remained in the supernatant (S). DM1A (anti-α-tubulin) and anti-UNC-119N (Tau and MAP2c) antibodies were used.