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Article

Intramembrane proteolysis by presenilin and presenilin-like proteases.

Journal of cell science - 15 Jul 2003

Xia Weiming, Wolfe Michael S

Abstract excerpt

Regulated intramembrane proteolysis is a novel mechanism involving proteases that hydrolyze their substrates in a hydrophobic environment. Presenilin (PS) 1 and PS 2 are required for intramembrane cleavage of an increasing number of type I membrane proteins, including the amyloid precursor protein of Alzheimer's disease and the Notch receptor, which signals during differentiation and development. Mutagenesis,...

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Source

Identifiers

PMID: 12808018
DOI: 10.1242/jcs.00651

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 6 Sept 2026. Manifest publication-graph-cohort-2026-09-06.1.

Source receipt: pubmed, retrieved 6 Sept 2026.

Related research

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Intramembrane proteolysis by presenilin and presenilin-like proteases.PMID 12808018Read ↗

Intramembrane proteolysis by presenilins.Semantic proximity Read ↗

Intramembrane proteolysis by gamma-secretase.Semantic proximity Read ↗

Identification of signal peptide peptidase, a presenilin-type aspartic protease.Semantic proximity Read ↗

Proteolytic Processing of Neuregulin 1 Type III by Three Intramembrane-cleaving Proteases.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 ↗

Presenilins mediate a dual intramembranous gamma-secretase cleavage of Notch-1.Semantic proximity Read ↗

Identification of a novel family of presenilin homologues.Semantic proximity Read ↗

The presenilins.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 ↗

Three-amino acid spacing of presenilin endoproteolysis suggests a general stepwise cleavage of gamma-secretase-mediated intramembrane proteolysis.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 ↗

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

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