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Article

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

The Journal of biological chemistry - 4 Jun 2004

Laudon Hanna, Karlström Helena, Mathews Paul M, Farmery Mark R, Gandy Samuel E, Lundkvist Johan, Lendahl Urban, Näslund Jan

Abstract excerpt

Processing of the Alzheimer amyloid precursor protein (APP) into the amyloid beta-protein and the APP intracellular domain is a proteolysis event mediated by the gamma-secretase complex where presenilin (PS) proteins are key constituents. PS is subjected to an endoproteolytic cleavage, generating a stable heterodimer composed of an N-terminal and a C-terminal fragment. Here we aimed at further understanding the...

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Source

Identifiers

PMID: 15051718
DOI: 10.1074/jbc.M401277200

Genes

APP

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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.

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Functional domains in presenilin 1: the Tyr-288 residue controls gamma-secretase activity and endoproteolysis.PMID 15051718Read ↗

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

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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 ↗

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