Moreno F J, Medina M, Pérez M, Montejo de Garcini E, Avila J
Centro de Biología Molecular Severo Ochoa, CSIC-UAM, Madrid, Spain.
FEBS Lett. 1995 Sep 18;372(1):65-8. doi: 10.1016/0014-5793(95)00934-2.
Tau protein, the major component of the aberrant structures termed paired helical filaments (PHFs) present in the brain of Alzheimer's disease patients, is pathologically phosphorylated in sites in and around the tubulin-binding sites. A single protein kinase, glycogen synthase kinase 3 (GSK 3), is able to phosphorylate tau at the flanking regions and, additionally, at the tubulin-binding motifs if heparin or tubulin is present. Serines-262 and -324 have been found to be modified at the tubulin-binding region of tau protein by GSK 3 in the presence of heparin or tubulin.
tau蛋白是阿尔茨海默病患者大脑中称为双螺旋丝（PHF）的异常结构的主要成分，在微管蛋白结合位点及其周围区域发生病理性磷酸化。单一蛋白激酶，即糖原合酶激酶3（GSK 3），能够在侧翼区域磷酸化tau蛋白，此外，如果存在肝素或微管蛋白，还能在微管蛋白结合基序处磷酸化。已发现，在肝素或微管蛋白存在的情况下，GSK 3会使tau蛋白微管蛋白结合区域的丝氨酸-262和-324发生修饰。
