The Alzheimer‐like phosphorylation of tau protein reduces microtubule binding and involves Ser‐Pro and Thr‐Pro motifs

FEBS Letters

Biernat, J.²  Meyer, H.E.³  Gustke, N.²  Mandelkow, E.-M.²  Goedert, M.¹  Steiner, B.²  Mandelkow, E.² 

[1] MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 2QH, UK;Max-Planck-Unit for Structural Molecular Biology, c/o DESY, Notkestraße 85, D-2000 Hamburg 52, Germany;Institut für Physiologische Chemie, Ruhr-Universität Bochum, Universitätsstr. 150, Geb. MA2/143, D-4630 Bochum, Germany

关键词: Tau protein;    Microtubule;    Alzheimer's disease;    Phosphorylation;    Proline-directed kinase;   

DOI  :  10.1016/0014-5793(92)80767-B

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown