Glycogen synthase kinase 3 phosphorylates recombinant human tau protein at serine‐262 in the presence of heparin (or tubulin)

FEBS Letters

Pérez, Mar¹  Avila, Jesús¹  Montejo de Garcini, Esteban¹  Medina, Miguel¹  Moreno, Francisco J.¹ 

[1] Centro de Biología Molecular ‘Severo Ochoa’, CSIC-UAM, Madrid, Spain

关键词: Tau phosphorylation;    Paired helical filament;    Alzheimer's disease;    GSK 3;    glycogen synthase kinase 3;    MAP;    microtubule associated protein;   

DOI  :  10.1016/0014-5793(95)00934-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown