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JCS ePress online publication date 9 Mar 2004
doi: 10.1242/jcs.01018

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Research Article

Role of tau phosphorylation by glycogen synthase kinase-3{beta} in the regulation of organelle transport


Yoshitaka Tatebayashi, Niloufar Haque, Yunn-Chyn Tung, Khalid Iqbal, and Inge Grundke-Iqbal*
* Author for correspondence (e-mail: i g iqbal{at}yahoo.com)

Anterograde organelle transport is known to be inhibited by overexpression of the microtubule-associated protein tau in cultured cells. However, the molecular mechanism regulating this function of tau protein has not previously been understood. We found that in PC12 cells treated with NGF or fibroblast growth factor-2, glycogen synthase kinase-3{beta} and tau were upregulated simultaneously from around day 2 of differentiation, with increasing glycogen synthase kinase-3-mediated tau phosphorylation. This phosphorylation did not alter tau's ability to bind to microtubules but appeared to be required for the maintenance of the anterograde organelle transport in differentiated cells. Lithium, alsterpaullone or valproate, three independent glycogen synthase kinase-3 inhibitors, but not butyrolactone 1, an inhibitor of cyclin-dependent protein kinases, induced mitochondrial clustering in association with tau dephosphorylation. In CHO cells transfected with human tau441, mitochondrial clustering was found in cells in which tau was unphosphorylated. These findings raise the possibility that the phosphorylation of tau by glycogen synthase kinase-3 might be involved in the regulation of organelle transport.
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