Dimeric Transmembrane Orientations of APP/C99 Regulate γ-Secretase Processing Line Impacting Signaling and Oligomerization.
Biochemistry
Biological Sciences
Molecular Biology
Neuroscience
Journal
iScience
ISSN: 2589-0042
Titre abrégé: iScience
Pays: United States
ID NLM: 101724038
Informations de publication
Date de publication:
18 Dec 2020
18 Dec 2020
Historique:
received:
14
09
2020
revised:
21
10
2020
accepted:
25
11
2020
entrez:
28
12
2020
pubmed:
29
12
2020
medline:
29
12
2020
Statut:
epublish
Résumé
Amyloid precursor protein (APP) cleavage by the β-secretase produces the C99 transmembrane (TM) protein, which contains three dimerization-inducing Gly-x-x-x-Gly motifs. We demonstrate that dimeric C99 TM orientations regulate the precise cleavage lines by γ-secretase. Of all possible dimeric orientations imposed by a coiled-coil to the C99 TM domain, the dimer containing the
Identifiants
pubmed: 33367225
doi: 10.1016/j.isci.2020.101887
pii: S2589-0042(20)31084-1
pmc: PMC7749410
doi:
Types de publication
Journal Article
Langues
eng
Pagination
101887Subventions
Organisme : NIA NIH HHS
ID : R01 AG027317
Pays : United States
Organisme : NIA NIH HHS
ID : RF1 AG027317
Pays : United States
Commentaires et corrections
Type : ErratumIn
Informations de copyright
© 2020 The Author(s).
Déclaration de conflit d'intérêts
S.N.C. is co-founder of Alsatech – Boston, MA and close family is owning stock in A.C. Immune Lausanne. The work of this manuscript is not linked to any current project at Alsatech or A.C. Immune, which are companies that work in the field of Alzheimer's disease.
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