Gustke N, Steiner B, Mandelkow E M, Biernat J, Meyer H E, Goedert M, Mandelkow E
Max-Planck-Unit for Structural Molecular Biology, c/o DESY, Hamburg, Germany.
FEBS Lett. 1992 Jul 28;307(2):199-205. doi: 10.1016/0014-5793(92)80767-b.
Tau protein can be transformed into an Alzheimer-like state by phosphorylation with a kinase activity from brain [Biernat et al. (1992) EMBO J. 11, 1593-1597]. Here we show that the phosphorylation at Ser-Pro motifs strongly decreases tau's affinity for microtubules. The major reduction occurs during the first of the three main stages of phosphorylation. The data explain the lower stability of microtubules resulting from the pathological tau phosphorylation.
通过用来自大脑的激酶活性进行磷酸化，tau蛋白可以转变为阿尔茨海默病样状态[比尔纳特等人（1992年）《欧洲分子生物学组织杂志》11卷，第1593 - 1597页]。在此我们表明，丝氨酸 - 脯氨酸基序处的磷酸化会显著降低tau与微管的亲和力。主要的降低发生在磷酸化三个主要阶段的第一个阶段。这些数据解释了病理性tau磷酸化导致的微管稳定性降低的原因。
