The function of the microtubule‐associated protein tau is variably modulated by graded changes in glycogen synthase kinase‐3β activity

FEBS Letters

Lovestone, S.²  Menu, R.¹  Brion, J.P.¹  Conreur, J.L.¹  Dayanandan, R.²  Anderton, B.H.²  Leroy, K.¹ 

[1] Laboratory of Pathology and Electron Microscopy, Université Libre de Bruxelles, School of Medecine, 808, route de Lennik, Bldg C-10, 1070 Brussels, Belgium;Department of Neuroscience, Institute of Psychiatry, De Crespigny Park, Denmark Hill, London SE5 8AF, UK

关键词: Tau;    Glycogen synthase kinase-3β;    Microtubule;    Cell process;    Phosphorylation;    Lithium;    GSK-3β;    glycogen synthase kinase-3β;    CHO;    Chinese hamster ovary;   

DOI  :  10.1016/S0014-5793(99)01720-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The microtubule-associated protein tau favors microtubule nucleation and stabilization and plays a role in the elongation of axons. We have investigated the ability of glycogen synthase kinase-3β (GSK-3β) to control tau-induced processes outgrowth. Tau-transfected Chinese hamster ovary (CHO) cells developed processes containing microtubule bundles after cytochalasin treatment, but a significant reduction in the number of cells harboring processes was observed in tau/GSK-3β-co-transfected cells. Lithium, an inhibitor of GSK-3β, counteracted in a dose-dependent manner this inhibitory effect of GSK-3β. These findings suggest that GSK-3β modulates in a graded manner the ability of tau to control the microtubule-dependent induction of cell processes.

【 授权许可】

Unknown