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

Published

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Huang, DY; Weisgraber, KH; Goedert, M; Saunders, AM; Roses, AD; Strittmatter, WJ

Published Date

  • June 16, 1995

Published In

Volume / Issue

  • 192 / 3

Start / End Page

  • 209 - 212

PubMed ID

  • 7566652

Pubmed Central ID

  • 7566652

International Standard Serial Number (ISSN)

  • 0304-3940

Digital Object Identifier (DOI)

  • 10.1016/0304-3940(95)11649-h

Language

  • eng

Conference Location

  • Ireland