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The function of the microtubule‐associated protein tau is variably modulated by graded changes in glycogen synthase kinase‐3β activity
Author(s) -
Leroy K.,
Menu R.,
Conreur J.L.,
Dayanandan R.,
Lovestone S.,
Anderton B.H.,
Brion J.P.
Publication year - 2000
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(99)01720-2
Subject(s) - gsk 3 , microtubule , chinese hamster ovary cell , microbiology and biotechnology , glycogen synthase , tau protein , transfection , tubulin , atp synthase , chemistry , protein kinase a , microtubule associated protein , phosphorylation , biology , biochemistry , enzyme , medicine , gene , receptor , disease , alzheimer's disease
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.