Tau‐tubulin kinase phosphorylates tau at Ser‐208 and Ser‐210, sites found in paired helical filament‐tau
Authors:
- Akira OmoriAOAkira Omori
- Atsuko OhtakeAOAtsuko Ohtake
- Kazuki SatoKSKazuki Sato
- Miho TakahashiMTMiho Takahashi
- 12 March 2001
- journal article
- Published by Wiley in FEBS Letters
- Vol. 492 (3) , 221-227
Abstract
Hyperphosphorylated tau protein is known to be a major component of the paired helical filaments (PHFs) that accumulate in the brain of Alzheimer's patients. The kinase that phosphorylated Ser‐208 and Ser‐210 in PHF‐tau had remained unknown. We used anti‐pS208 and anti‐pS210 antibodies and Western blots to confirm that the tau‐tubulin kinase (TTK) phosphorylates tau at Ser‐208 and at Ser‐210. Using partial amino acid sequences of purified bovine brain TTK, a mouse cDNA of TTK was isolated and the sequence was determined. Its 963 bp coding region is composed of 320 amino acids and encodes a 36 kDa protein indistinguishable in size from authentic bovine brain TTK. Our immunoblot analysis demonstrated that TTK is ubiquitously distributed in the rat tissues, and that it is developmentally regulated in the rat brain.Keywords
This publication has 25 references indexed in Scilit:
- Phosphorylation Sites on Tau Identified by Nanoelectrospray Mass SpectrometryJournal of Neurochemistry, 2000
- Phosphorylation of tau protein by recombinant GSK‐3β: pronounced phosphorylation at select Ser/Thr‐Pro motifs but no phosphorylation at Ser262 in the repeat domainFEBS Letters, 1999
- Sequential phosphorylation of Tau by glycogen synthase kinase‐3β and protein kinase A at Thr212 and Ser214 generates the Alzheimer‐specific epitope of antibody AT100 and requires a paired‐helical‐filament‐like conformationEuropean Journal of Biochemistry, 1998
- A novel tau‐tubulin kinase from bovine brainFEBS Letters, 1995
- Rapid Alzheimer‐like phosphorylation of tau by the synergistic actions of non‐proline‐dependent protein kinases and GSK‐3FEBS Letters, 1995
- Modulation of GSK‐3‐catalyzed phosphorylation of microtubule‐associated protein tau by non‐proline‐dependent protein kinasesFEBS Letters, 1995
- Localization and Developmental Changes of τ Protein Kinase I/Glycogen Synthase Kinase‐3β in Rat BrainJournal of Neurochemistry, 1994
- τ Protein Kinase II Is Involved in the Regulation of the Normal Phosphorylation State of τ ProteinJournal of Neurochemistry, 1993
- The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic DomainsScience, 1988
- A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye bindingAnalytical Biochemistry, 1976