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Article

Mutations at the P1' position of Notch1 decrease intracellular domain stability rather than cleavage by gamma-secretase.

Biochemical and biophysical research communications - 13 Dec 2002

Blat Yuval, Meredith Jere E, Wang Qian, Bradley Jodi D, Thompson Lorin A, Olson Richard E, Stern Andrew M, Seiffert Dietmar

Abstract excerpt

Gamma-secretase is a unique protease which cleaves within the transmembrane domain of several substrate proteins. Among gamma-secretase substrates are members of the Notch family of receptors and the amyloid precursor protein. In this study we used a cell-free Notch-cleavage assay and specific gamma-secretase inhibitors to study the cleavage of Notch by gamma-secretase. Using this assay, we found that, in...

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Source

Identifiers

PMID: 12459176
DOI: 10.1016/s0006-291x(02)02705-5

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Mutations at the P1' position of Notch1 decrease intracellular domain stability rather than cleavage by gamma-secretase.PMID 12459176Read ↗

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 ↗

Effects of transmembrane phenylalanine residues on γ-secretase-mediated Notch-1 proteolysisSemantic proximity Read ↗

γ-Secretase-mediated endoproteolysis of neuregulin-1 and E-cadherinSemantic proximity Read ↗

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

A sensitive and quantitative assay for measuring cleavage of presenilin substrates.Semantic proximity Read ↗

Analysis of transmembrane domain mutants is consistent with sequential cleavage of Notch by gamma-secretase.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 ↗

Important functional role of residue x of the presenilin GxGD protease active site motif for APP substrate cleavage specificity and substrate selectivity of γ-secretase.Semantic proximity Read ↗

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

Catalytic Site-Directed γ-Secretase Complex Inhibitors Do Not Discriminate Pharmacologically between Notch S3 and β-APP CleavagesSemantic proximity Read ↗

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

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