Abstract:
:Tungstate treatment increases the phosphorylation of glycogen synthase kinase-3beta (GSK3beta) at serine 9, which triggers its inactivation both in cultured neural cells and in vivo. GSK3 phosphorylation is dependent on the activation of extracellular signal-regulated kinases 1/2 (ERK1/2) induced by tungstate. As a consequence of GSK3 inactivation, the phosphorylation of several GSK3-dependent sites of the microtubule-associated protein tau decreases. Tungstate reduces tau phosphorylation only in primed sequences, namely, those prephosphorylated by other kinases before GSK3beta modification, which are serines 198, 199, or 202 and threonine 231. The phosphorylation at these sites is involved in reduction of the interaction of tau with microtubules that occurs in Alzheimer's disease.
journal_name
J Neurosci Resjournal_title
Journal of neuroscience researchauthors
Gómez-Ramos A,Domínguez J,Zafra D,Corominola H,Gomis R,Guinovart JJ,Avila Jdoi
10.1002/jnr.20726keywords:
subject
Has Abstractpub_date
2006-02-01 00:00:00pages
264-73issue
2eissn
0360-4012issn
1097-4547journal_volume
83pub_type
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