Ontology highlight
ABSTRACT:
SUBMITTER: Payne AJ
PROVIDER: S-EPMC3843983 | biostudies-literature | 2013 Dec
REPOSITORIES: biostudies-literature
Payne Andrew J AJ Gerdes Bryan C BC Naumchuk Yuliya Y McCalley Audrey E AE Kaja Simon S Koulen Peter P
Experimental neurology 20130909
Presenilins (PS), endoplasmic reticulum (ER) transmembrane proteins, form the catalytic core of γ-secretase, an amyloid precursor protein processing enzyme. Mutations in PS lead to Alzheimer's disease (AD) by altering γ-secretase activity to generate pathologic amyloid beta and amyloid plaques in the brain. Here, we identified a novel mechanism where binding of a soluble, cytosolic N-terminal domain fragment (NTF) of PS to intracellular Ca(2+) release channels, ryanodine receptors (RyR), control ...[more]