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

作者信息

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

机构信息

Laboratory of Pathology and Electron Microscopy, Universit¿e Libre de Bruxelles, School of Medecine, 808, route de Lennik, Bldg C-10, 1070, Brussels, Belgium.

出版信息

FEBS Lett. 2000 Jan 7;465(1):34-8. doi: 10.1016/s0014-5793(99)01720-2.

Abstract

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-3beta (GSK-3beta) 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-3beta-co-transfected cells. Lithium, an inhibitor of GSK-3beta, counteracted in a dose-dependent manner this inhibitory effect of GSK-3beta. These findings suggest that GSK-3beta modulates in a graded manner the ability of tau to control the microtubule-dependent induction of cell processes.

摘要

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