ApoE3 binding to tau tandem repeat I is abolished by tau serine262 phosphorylation

Neurosci Lett. 1995 Jun 16;192(3):209-12. doi: 10.1016/0304-3940(95)11649-h.


The risk of Alzheimer's disease is determined, in part, by inheritance of specific alleles of ApoE. Isoform specific interactions of ApoE have been shown with the microtubule-associated protein tau, which forms the neurofibrillary tangle in this disease. Synthetic peptides representing each of the four microtubule-binding domains of tau more avidly bind ApoE3 than ApoE4. Phosphorylation of serine262 in domain I of tau decreases tau binding to microtubules and also abolishes binding by ApoE3. Understanding the molecular mechanisms of the high avidity, isoform-specific interactions of ApoE with tau may help in developing approaches for disease intervention.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Alzheimer Disease / metabolism
  • Amino Acid Sequence
  • Apolipoprotein E3
  • Apolipoproteins E / metabolism*
  • Humans
  • Molecular Sequence Data
  • Phosphorylation
  • Protein Binding / physiology
  • Serine / metabolism*
  • tau Proteins / metabolism*
  • tau Proteins / ultrastructure


  • Apolipoprotein E3
  • Apolipoproteins E
  • tau Proteins
  • Serine