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PKA modulates GSK‐3β‐ and cdk5‐catalyzed phosphorylation of tau in site‐ and kinase‐specific manners
Abstract
Phosphorylation of tau protein is regulated by several kinases, especially glycogen synthase kinase 3β (GSK‐3β), cyclin‐dependent protein kinase 5 (cdk5) and cAMP‐dependent protein kinase (PKA). Phosphorylation of tau by PKA primes it for phosphorylation by GSK‐3β, but the site‐specific modulation of GSK‐3β‐catalyzed tau phosphorylation by the prephosphorylation has not been well investigated. Here, we found that prephosphorylation by PKA promotes GSK‐3β‐catalyzed tau phosphorylation at Thr181, Ser199, Ser202, Thr205, Thr217, Thr231, Ser396 and Ser422, but inhibits its phosphorylation at Thr212 and Ser404. In contrast, the prephosphorylation had no significant effect on its subsequent phosphorylation by cdk5 at Thr181, Ser199, Thr205, Thr231 and Ser422; inhibited it at Ser202, Thr212, Thr217 and Ser404; and slightly promoted it at Ser396. These studies reveal the nature of the inter‐regulation of tau phosphorylation by the three major tau kinases.
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“In case of Tau phosphorylated by GSK3β, about 50% of the molecules remained non‐phosphorylated, and a second prominent phospho‐species occurred, similar to previous observations (Liu et al, 2006).”
From Molecular crowding and RNA synergize to promote phase separation, microtubule interaction, and seeding of Tau condensates (2022) · cites this paper as Liu et al, 2006
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Self-citationMonoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
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“phosphorylated Ser396 than to phosphorylated Ser404 of tau [26].”
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Self-citationGlycogen Synthase Kinase 3β Phosphorylates Tau at Both Primed and Unprimed Sites
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Metadata
- Authors
- Liu, F., Liang, Z., Shi, J., Yin, D., El-Akkad, E., Grundke-Iqbal, I., Iqbal, K., & Gong, C.-X.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2006-10-24
- Volume
- 580
- Issue
- 26
- Pages
- 6269-6274
- ISSN
- 0014-5793
- 1873-3468
- Cited by
- 138
- References
- 6
- Language
- en
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