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Presenilin structure, function and role in Alzheimer disease

journal contribution
posted on 2023-06-08, 09:11 authored by Paul E Fraser, Dun-Sheng Yang, Gang Yu, Lyne Lévesque, Masaki Nishimura, Shigeki Arawaka, Louise SerpellLouise Serpell, Ekaterina Rogaeva, Peter St George-Hyslop
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 ß-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 ß-peptides. Furthermore, presenilins interact with ß-catenin to form presenilin complexes, and the physiological and mutational effects are also observed in the catenin signal transduction pathway.

History

Publication status

  • Published

Journal

BBA - Molecular Basis of Disease

ISSN

0925-4439

Publisher

Elsevier

Issue

1

Volume

1502

Department affiliated with

  • Biochemistry Publications

Full text available

  • No

Peer reviewed?

  • Yes

Legacy Posted Date

2012-02-06

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