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Article

Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.

The Journal of cell biology - 5 Aug 2002

Kaether Christoph, Lammich Sven, Edbauer Dieter, Ertl Michaela, Rietdorf Jens, Capell Anja, Steiner Harald, Haass Christian

Abstract excerpt

Amyloid beta-peptide (Abeta) is generated by the consecutive cleavages of beta- and gamma-secretase. The intramembraneous gamma-secretase cleavage critically depends on the activity of presenilins (PS1 and PS2). Although there is evidence that PSs are aspartyl proteases with gamma-secretase activ...

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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: 12147673
DOI: 10.1083/jcb.200201123
PMCID: PMC2173840

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 1 Sept 2026. Prepared record publication-12147673-2026-09-01.1. Manifest publication-graph-cohort-2026-09-01.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 1 Sept 2026.

Related research

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Presenilin-1 affects trafficking and processing of betaAPP and is targeted in a complex with nicastrin to the plasma membrane.PMID 12147673Read ↗

Cell surface presenilin-1 participates in the gamma-secretase-like proteolysis of Notch.Semantic proximity Read ↗

The levels of mature glycosylated nicastrin are regulated and correlate with gamma-secretase processing of amyloid beta-precursor protein.Semantic proximity Read ↗

Intramembrane proteolysis by gamma-secretase.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 ↗

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

Role of presenilin in gamma-secretase cleavage of amyloid precursor protein.Semantic proximity Read ↗

Presenilin-1-mediated retention of APP derivatives in early biosynthetic compartments.Semantic proximity Read ↗

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

Intramembrane proteolysis by presenilin and presenilin-like proteases.Semantic proximity Read ↗

Activation and intrinsic gamma-secretase activity of presenilin 1.Semantic proximity Read ↗

Interactome analyses of mature γ-secretase complexes reveal distinct molecular environments of presenilin (PS) paralogs and preferential binding of signal peptide peptidase to PS2.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 ↗

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