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Article

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

Neurobiology of aging - 1 Feb 2012

Chiang Po-Min, Fortna Ryan R, Price Donald L, Li Tong, Wong Philip C

Abstract excerpt

γ-Secretase, a multisubunit transmembrane protease comprised of presenilin, nicastrin, presenilin enhancer 2, and anterior pharynx-defective one, participates in the regulated intramembrane proteolysis of Type I membrane proteins including the amyloid precursor protein (APP). Although Aph-1 is thought to play a structural role in the assembly of γ-secretase complex and several transmembrane domains (TMDs) of...

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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Identifiers

PMID: 20382452
DOI: 10.1016/j.neurobiolaging.2009.12.028
PMCID: PMC2904414

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026.

Related research

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Click a neighbor to travelStep 1 · 12 closest

Specific domains in anterior pharynx-defective 1 determine its intramembrane interactions with nicastrin and presenilin.PMID 20382452Read ↗

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

APH-1a Is the Principal Mammalian APH-1 Isoform Present in γ-Secretase Complexes during Embryonic DevelopmentSemantic proximity Read ↗

Aph-1 contributes to the stabilization and trafficking of the gamma-secretase complex through mechanisms involving intermolecular and intramolecular interactions.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 ↗

Membrane topology and nicastrin-enhanced endoproteolysis of APH-1, a component of the gamma-secretase complex.Semantic proximity Read ↗

Presenilin-1 D257A and D385A mutants fail to cleave Notch in their endoproteolyzed forms, but only presenilin-1 D385A mutant can restore its gamma-secretase activity with the compensatory overexpression of normal C-terminal fragment.Semantic proximity Read ↗

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

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

Negative evidence for a role of APH1B T27I variant in Alzheimer's disease.Semantic proximity Read ↗

Polar transmembrane-based amino acids in presenilin 1 are involved in endoplasmic reticulum localization, Pen2 protein binding, and γ-secretase complex stabilization.Semantic proximity Read ↗

Characterization of APH-1 mutants with a disrupted transmembrane GxxxG motif.Semantic proximity Read ↗

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