Presenilin structure, function and role in Alzheimer disease

Paul E. Fraser, Dun Sheng Yang, Gang Yu, Lyne Lévesque, Masaki Nishimura, Shigeki Arawaka, Louise C. Serpell, Ekaterina Rogaeva, Peter St George-Hyslop

Research output: Contribution to journalReview articlepeer-review

90 Scopus citations


Numerous missense mutations in the presenilins are associated with the autosomal dominant form of familial Alzheimer disease. Presenilin genes encode polytopic transmembrane proteins, which are processed by proteolytic cleavage and form high-molecular-weight complexes under physiological conditions. The presenilins have been suggested to be functionally involved in developmental morphogenesis, unfolded protein responses and processing of selected proteins including the β-amyloid precursor protein. Although the underlying mechanism by which presenilin mutations lead to development of Alzheimer disease remains elusive, one consistent mutational effect is an overproduction of long-tailed amyloid β-peptides. Furthermore, presenilins interact with β-catenin to form presenilin complexes, and the physiological and mutational effects are also observed in the catenin signal transduction pathway. Copyright (C) 2000 Elsevier Science B.V.

Original languageEnglish (US)
Pages (from-to)1-15
Number of pages15
JournalBiochimica et Biophysica Acta - Molecular Basis of Disease
Issue number1
StatePublished - Jul 26 2000


  • Alzheimer disease
  • Amyloid-β peptide
  • Armadillo
  • Notch 1
  • Presenilin
  • Secretase
  • Tau
  • β-Amyloid precursor protein
  • β-Catenin

ASJC Scopus subject areas

  • Molecular Medicine
  • Molecular Biology


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