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Article

Evidence That the "Lid" Domain of Nicastrin Is Not Essential for Regulating γ-Secretase Activity.

The Journal of biological chemistry - 25 Mar 2016

Zhang Xulun, Sullivan Eric, Scimeca Maggie, Wu Xianzhong, Li Yue-Ming, Sisodia Sangram S

Abstract excerpt

Understanding of the structure of the γ-secretase complex consisting of presenilin (PS), anterior pharynx-defective 1 (APH-1), nicastrin (NCT), and presenilin enhancer 2 (PEN-2) is of significant therapeutic interest for the design of γ-secretase modulators for Alzheimer disease. The structure of γ-secretase revealed by cryo-EM approaches suggested a substrate binding mechanism for NCT, a bilobar structure that...

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Share to Amyloid Precursor Protein Secretases
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Source

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Identifiers

PMID: 26887941
DOI: 10.1074/jbc.C115.701649
PMCID: PMC4807262

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Evidence That the "Lid" Domain of Nicastrin Is Not Essential for Regulating γ-Secretase Activity.PMID 26887941Read ↗

An atomic structure of human γ-secretase.Semantic proximity Read ↗

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

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

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

Intramembrane proteolysis by gamma-secretase.Semantic proximity Read ↗

C-terminal PAL motif of presenilin and presenilin homologues required for normal active site conformation.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 ↗

Pen-2 is essential for γ-secretase complex stability and trafficking but partially dispensable for endoproteolysis.Semantic proximity Read ↗

Nicastrin binds to membrane-tethered Notch.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 ↗

Conditional inactivation of nicastrin restricts amyloid deposition in an Alzheimer's disease mouse model.Semantic proximity Read ↗

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

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