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Article

Presenilin endoproteolysis is an intramolecular cleavage.

Molecular and cellular neurosciences - 1 May 2005

Brunkan Anne L, Martinez Maribel, Walker Emily S, Goate Alison M

Abstract excerpt

Mutations in the presenilin genes (PS) account for most cases of familial Alzheimer's disease. PS contain the active site of the gamma-secretase complex that cleaves within the transmembrane domain of beta-amyloid precursor protein (APP). Full-length PS undergoes regulated endoproteolysis to produce fragments that comprise the active form of PS. The "presenilinase" responsible for endoproteolysis is unknown but...

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Source

Identifiers

PMID: 15866047
DOI: 10.1016/j.mcn.2004.12.012

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Presenilin endoproteolysis is an intramolecular cleavage.PMID 15866047Read ↗

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

Functional domains in presenilin 1: the Tyr-288 residue controls gamma-secretase activity and endoproteolysis.Semantic proximity Read ↗

Amyloidogenic function of the Alzheimer's disease-associated presenilin 1 in the absence of endoproteolysis.Semantic proximity Read ↗

Endoproteolysis of presenilin in vitro: inhibition by gamma-secretase inhibitors.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 ↗

Pathogenic Aβ production by heterozygous PSEN1 mutations is intrinsic to the mutant protein and not mediated by conformational hindrance of wild-type PSEN1.Semantic proximity Read ↗

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

Mutational analysis of intrinsic regions of presenilin 2 that determine its endoproteolytic cleavage and pathological function.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 ↗

Presenilin 1 mutations activate gamma 42-secretase but reciprocally inhibit epsilon-secretase cleavage of amyloid precursor protein (APP) and S3-cleavage of notch.Semantic proximity Read ↗

Alzheimer presenilin-1 mutations dramatically reduce trimming of long amyloid β-peptides (Aβ) by γ-secretase to increase 42-to-40-residue Aβ.Semantic proximity Read ↗

Presenilin clinical mutations can affect gamma-secretase activity by different mechanisms.Semantic proximity Read ↗

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