Roses, Allen D

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

D Y Huang; K H Weisgraber; M Goedert; A M Saunders; A D Roses; W J Strittmatter (Profiled Authors: Roses, Allen D; Strittmatter, Warren J; Saunders, Ann M; Goedert, Michel)

Department of Medicine (Neurology), Joseph and Kathleen Bryan Alzheimer's Disease Research Center, Duke University Medical Center, Durham, NC 27710, USA.
Neuroscience letters 1995;192(3):209-12.

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.

1 Originating Grant

• 1.

  ROSES, ALLEN D

  GENETICS OF LATE AND EARLY ONSET ALZHEIMERS DISEASE

  1 August 1988 - 31 July 1996

  NATIONAL INSTITUTE ON AGING

  Total Funding: $ 5,327,551

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