Journal
NEUROSCIENCE LETTERS
Volume 312, Issue 3, Pages 141-144Publisher
ELSEVIER SCI IRELAND LTD
DOI: 10.1016/S0304-3940(01)02206-6
Keywords
tau; glycogen synthase kinase 3 beta; microtubules; phosphorylation; neuron
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Tau is a neuronal microtubule-associated protein found predominantly in axons. Hyperphosphorylation of tau reduces the stability of microtubules, which may be a pathogenic mechanism in Alzheimer's disease. To understand the different effects between tau and glycogen synthase kinase 3 beta (GSK-3 beta) phosphorylated tau on the organization and stability of microtubules, we performed transfection studies on 3T3 cells using EGFP-tau (Enhanced Green Fluorescence Protein-au) and GSK-3 beta to quantify the stability of microtubules. Laser confocal microscope observation revealed that thick and thin microtubule bundles could be induced by-tau and GSK-3 beta phosphorylated tau. The bundles appeared either to be relatively straight or to form a ring around the circumference of the cell. Both the thick and thin microtubule bundles were resistant to colchicine-induced dissociation, with thick bundles more resistant than thin bundles. The bundles induced by GSK-3 beta phosphorylated tau were sensitive to colchicine, and could be reversed by the addition of LiCl, an inhibitor of GSK-3 beta. (C) 2001 Elsevier Science Ireland Ltd. All rights reserved.
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