Structure-activity relationship of presenilin in γ-secretase-mediated intramembrane cleavage.
Alzheimer disease
Intramembrane protease
Proteolysis
Structure
γ-Secretase
Journal
Seminars in cell & developmental biology
ISSN: 1096-3634
Titre abrégé: Semin Cell Dev Biol
Pays: England
ID NLM: 9607332
Informations de publication
Date de publication:
09 2020
09 2020
Historique:
received:
23
09
2019
revised:
18
02
2020
accepted:
19
02
2020
pubmed:
17
3
2020
medline:
25
6
2021
entrez:
16
3
2020
Statut:
ppublish
Résumé
Genetic research on familial cases of Alzheimer disease have identified presenilin (PS) as an important membrane protein in the pathomechanism of this disease. PS is the catalytic subunit of γ-secretase, which is responsible for the generation of amyloid-β peptide deposited in the brains of Alzheimer disease patients. γ-Secretase is an atypical protease composed of four membrane proteins (i.e., presenilin, nicastrin, anterior pharynx defective-1 (Aph-1), and presenilin enhancer-2 (Pen-2)) and mediates intramembrane proteolysis. Numerous investigations have been conducted toward understanding the structural features of γ-secretase components as well as the cleavage mechanism of γ-secretase. In this review, we summarize our current understanding of the structure and activity relationship of the γ-secretase complex.
Identifiants
pubmed: 32171519
pii: S1084-9521(18)30291-X
doi: 10.1016/j.semcdb.2020.02.006
pii:
doi:
Substances chimiques
Membrane Proteins
0
Presenilins
0
Amyloid Precursor Protein Secretases
EC 3.4.-
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Review
Langues
eng
Sous-ensembles de citation
IM
Pagination
102-109Informations de copyright
Copyright © 2020 Elsevier Ltd. All rights reserved.