Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding.

Abstract

Glycogen synthase kinase 3beta (GSK3beta) phosphorylates substrates, including the microtubule-associated protein tau, at both primed and unprimed epitopes. GSK3beta phosphorylation of tau negatively regulates tau-microtubule interactions; however the differential effects of phosphorylation at primed and unprimed epitopes on tau is unknown. To examine the… (More)

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Cite this paper

@article{Cho2003GlycogenSK, title={Glycogen synthase kinase 3beta phosphorylates tau at both primed and unprimed sites. Differential impact on microtubule binding.}, author={Jae-Hyeon Cho and Gail V. W. Johnson}, journal={The Journal of biological chemistry}, year={2003}, volume={278 1}, pages={187-93} }