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Article

Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations.

The Journal of biological chemistry - 8 May 2009

Futai Eugene, Yagishita Sosuke, Ishiura Shoichi

Abstract excerpt

gamma-Secretase is a multisubunit membrane protein complex consisting of presenilin (PS1), nicastrin (NCT), anterior pharynx-1, and presenilin enhancer 2. To analyze the activity of familial Alzheimer disease mutants and to understand the roles of the subunits, we established a yeast transcriptional activator Gal4p system with artificial gamma-secretase substrates containing amyloid precursor protein or Notch...

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Share to Amyloid beta-Protein Precursor
Share to Amyloid Precursor Protein Secretases

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Immunoblotting

Share to Membrane Glycoproteins

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Share to Receptors, Cell Surface

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Source

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Identifiers

PMID: 19254953
DOI: 10.1074/jbc.M807653200
PMCID: PMC2676034

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Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations.PMID 19254953Read ↗

Saccharomyces cerevisiae Models of Alzheimer's Disease to Screen Genes, Mutations, and Chemicals Affecting Amyloid Beta Production by γ-Secretase.Semantic proximity Read ↗

Mutations in nicastrin protein differentially affect amyloid beta-peptide production and Notch protein processing.Semantic proximity Read ↗

Positive and negative regulation of the gamma-secretase activity by nicastrin in a murine model.Semantic proximity Read ↗

Nicastrin interacts with gamma-secretase complex components via the N-terminal part of its transmembrane domain.Semantic proximity Read ↗

Co-expression of nicastrin and presenilin rescues a loss of function mutant of APH-1.Semantic proximity Read ↗

Specific Mutations in Aph1 Cause γ-Secretase Activation.Semantic proximity Read ↗

Characterization of the reconstituted gamma-secretase complex from Sf9 cells co-expressing presenilin 1, nicastrin [correction of nacastrin], aph-1a, and pen-2.Semantic proximity Read ↗

Presenilins mutated at Asp-257 or Asp-385 restore Pen-2 expression and Nicastrin glycosylation but remain catalytically inactive in the absence of wild type Presenilin.Semantic proximity Read ↗

Mutation analysis of the presenilin 1 N-terminal domain reveals a broad spectrum of gamma-secretase activity toward amyloid precursor protein and other substrates.Semantic proximity Read ↗

Specific domains in anterior pharynx-defective 1 determine its intramembrane interactions with nicastrin and presenilin.Semantic proximity Read ↗

Alzheimer's disease-linked mutations in presenilin-1 result in a drastic loss of activity in purified γ-secretase complexes.Semantic proximity Read ↗

Nicastrin is required for assembly of presenilin/gamma-secretase complexes to mediate Notch signaling and for processing and trafficking of beta-amyloid precursor protein in mammals.Semantic proximity Read ↗

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