Nuclear signalling by membrane protein intracellular domains: The AICD enigma

被引：66

作者：

Beckett, Caroline ^{[1
]}

Nalivaeva, Natalia N. ^{[1
,2
]}

Belyaev, Nikolai D. ^{[1
]}

Turner, Anthony J. ^{[1
]}

机构：

[1] Univ Leeds, Fac Biol Sci, Inst Mol & Cellular Biol, Leeds LS2 9JT, W Yorkshire, England

[2] IM Sechenov Inst Evolutionary Physiol & Biochem R, St Petersburg, Russia

来源：

CELLULAR SIGNALLING | 2012年 / 24卷 / 02期

基金：

英国医学研究理事会;

关键词：

AICD; Alzheimer's disease; Amyloid; Intramembrane proteolysis; Neprilysin; Secretase; AMYLOID-PRECURSOR-PROTEIN; REGULATED INTRAMEMBRANE PROTEOLYSIS; DEPENDENT GAMMA-SECRETASE; C-TERMINAL FRAGMENTS; ALZHEIMERS-DISEASE; GENE-EXPRESSION; ALPHA-SECRETASE; A-BETA; TRANSCRIPTIONAL CONTROL; CYTOSKELETAL DYNAMICS;

D O I：

10.1016/j.cellsig.2011.10.007

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Alzheimer's disease (AD) is a neurodegenerative illness and the leading cause of dementia in the elderly. The accumulation of amyloid-beta peptide (A beta) is a well-known pathological hallmark associated with the disease. However, A beta is only one of several metabolites produced by beta- and gamma-secretase actions on the transmembrane protein, the amyloid precursor protein (APP). A proteolytic fragment termed the APP intracellular domain (AICD) is also produced. By analogy with the Notch signalling pathway, AICD has been proposed as a transcriptional regulator although its mechanism of action and the complement of genes regulated remain controversial. This review will focus on the contributions that studies of APP processing have brought to the understanding of a novel nuclear signalling pathway that may contribute to the pathology of AD and may provide new therapeutic opportunities. (C) 2011 Elsevier Inc. All rights reserved.

引用

页码：402 / 409

页数：8

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