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Article

Moonlighting activity of presenilin in plants is independent of gamma-secretase and evolutionarily conserved.

Proceedings of the National Academy of Sciences of the United States of America - 14 Aug 2007

Khandelwal Abha, Chandu Dilip, Roe Catherine M, Kopan Raphael, Quatrano Ralph S

Abstract excerpt

Presenilins (PS) provide the catalytic activity for gamma-secretase, which cleaves physiologically relevant substrates including Notch, ErbB4, and APP. Recent genetic studies indicated that the contribution of PS1 to mouse development includes gamma-secretase-independent functions that cannot be easily explained by any of the demonstrated or hypothesized functions of this protein. To begin a nonbiased analysis of...

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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: 17684101
DOI: 10.1073/pnas.0702038104
PMCID: PMC1948938

Genes

APP

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 5 Sept 2026. Manifest publication-graph-cohort-2026-09-05.1.

Source receipt: pubmed, retrieved 5 Sept 2026.

Related research

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Moonlighting activity of presenilin in plants is independent of gamma-secretase and evolutionarily conserved.PMID 17684101Read ↗

Identification of presenilin mutations that have sufficient gamma-secretase proteolytic activity to mediate Notch signaling but disrupt organelle and neuronal healthSemantic proximity Read ↗

The physiological role of presenilins in cellular differentiation: lessons from model organisms.Semantic proximity Read ↗

The mechanism of gamma-secretase activities through high molecular weight complex formation of presenilins is conserved in Drosophila melanogaster and mammals.Semantic proximity Read ↗

Generation and Characterization of a Novel Knockin Mouse Model Expressing PSEN1 D385A: Implications for Investigating Herbal Drug Effects in γ-Secretase Activity.Semantic proximity Read ↗

Presenilin 1 negatively regulates beta-catenin/T cell factor/lymphoid enhancer factor-1 signaling independently of beta-amyloid precursor protein and notch processing.Semantic proximity Read ↗

Dictyostelium possesses highly diverged presenilin/gamma-secretase that regulates growth and cell-fate specification and can accurately process human APP: a system for functional studies of the presenilin/gamma-secretase complex.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 ↗

Presenilins: Genes for Life and DeathSemantic proximity Read ↗

Presenilin-interacting proteinsSemantic proximity Read ↗

Presenilins, processing of beta-amyloid precursor protein, and notch signaling.Semantic proximity Read ↗

Nicastrin is dispensable for gamma-secretase protease activity in the presence of specific presenilin mutations.Semantic proximity Read ↗

Presenilins: molecular switches between proteolysis and signal transductionSemantic proximity Read ↗

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