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The physiology of the β‐amyloid precursor protein intracellular domain AICD

Pardossi‐Piquard, Raphaëlle, Checler, Frédéric·2012·Journal of Neurochemistry

Abstract

J. Neurochem. (2012) 120 (Suppl. 1), 109–124. The amyloid‐β precursor protein (βAPP) undergoes several cleavages by enzymatic activities called secretases. Numerous studies aimed at studying the biogenesis and catabolic fate of Aβ peptides, the proteinaceous component of the senile plaques that accumulate in Alzheimer’s disease‐affected brains. Relatively recently, another secretase‐mediated β‐APP‐derived catabolite called APP IntraCellular Domain (AICD) entered the game. Whether AICD corresponded to a biologically inert by‐pass product of βAPP processing or whether it could harbor its own function remained questionable. In this study, we review the mechanisms by which AICD is generated and how its production is regulated. Furthermore, we discuss the degradation mechanism underlying its rapid catabolic fate. Finally, we review putative AICD‐related functions and more particularly, the numerous studies indicating that AICD could translocate to the nucleus and control at a transcriptional level, the expression of a series of proteins involved in various functions including the control of cell death and Aβ degradation.

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Metadata

Authors
Pardossi‐Piquard, R., & Checler, F.
Venue
Journal of Neurochemistry
Publisher
Wiley
Published
2011-11-28
Volume
120
Issue
s1
Pages
109-124
ISSN
  • 0022-3042
  • 1471-4159
Cited by
159
References
14
Language
en

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