Effect of phosphorylation on interaction of human tau protein with 14-3-3zeta

Biochem Biophys Res Commun. 2009 Feb 20;379(4):990-4. doi: 10.1016/j.bbrc.2008.12.164. Epub 2009 Jan 10.


Interaction of the shortest isoform of tau protein (tau3) with human 14-3-3zeta was analyzed by means of native gel electrophoresis, chemical crosslinking and size-exclusion chromatography. Phosphorylation by cAMP-dependent protein kinase (up to 2 mole of phosphate per mole of tau3) strongly enhanced interaction of tau3 with 14-3-3. Apparent K(D) of the complexes formed by phosphorylated tau3 and 14-3-3 was close to 2 microM, whereas the corresponding constant for unphosphorylated tau3 was at least 10 times higher. The stoichiometry of the complexes formed by phosphorylated tau3 and 14-3-3 was variable and was different from 1:1. 14-3-3 decreased the probability of formation of chemically crosslinked large homooligomers of phosphorylated tau3 and at the same time induced formation of crosslinked heterooligomeric complexes of tau3 and 14-3-3 with an apparent molecular mass of 120-140 kDa.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • 14-3-3 Proteins / chemistry
  • 14-3-3 Proteins / metabolism*
  • Chromatography, Gel
  • Cross-Linking Reagents / chemistry
  • Cyclic AMP-Dependent Protein Kinases / chemistry
  • Cyclic AMP-Dependent Protein Kinases / metabolism
  • Electrophoresis
  • Humans
  • Phosphorylation
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism
  • tau Proteins / chemistry
  • tau Proteins / metabolism*


  • 14-3-3 Proteins
  • Cross-Linking Reagents
  • Protein Isoforms
  • tau Proteins
  • Cyclic AMP-Dependent Protein Kinases