A serine/threonine proline kinase activity is included in the tau protein kinase fraction forming a paired helical filament epitope

Neurosci Lett. 1991 Jul 22;128(2):195-8. doi: 10.1016/0304-3940(91)90259-v.


Previously we partially purified a novel protein kinase which phosphorylated tau and formed a paired helical filament (PHF) epitope. In this paper we show that the kinase fraction contains a protein kinase activity recognizing serine/threonine proline sequence. The kinase phosphorylated tau at the tau-1 site previously reported as one of the phosphorylation sites on PHF by other groups. The kinase also phosphorylated extraordinarily insoluble portion located on C-terminal region of tau in PHF. It is worth considering that tau phosphorylated by this kinase activity is incorporated into PHF.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Brain / enzymology*
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cattle
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Kinases / metabolism*
  • Serine / metabolism
  • Threonine / metabolism
  • tau Proteins / metabolism*


  • tau Proteins
  • Threonine
  • Serine
  • Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases