Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and βAPP processing View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

2000-09

AUTHORS

Gang Yu, Masaki Nishimura, Shigeki Arawaka, Diane Levitan, Lili Zhang, Anurag Tandon, You-Qiang Song, Ekaterina Rogaeva, Fusheng Chen, Toshitaka Kawarai, Agnes Supala, Lyne Levesque, Haung Yu, Dun-Sheng Yang, Erin Holmes, Paul Milman, Yan Liang, Dong Mei Zhang, Dong Hong Xu, Christine Sato, Evgeny Rogaev, Marsha Smith, Christopher Janus, Yanni Zhang, Ruedi Aebersold, Lindsay Farrer, Sandro Sorbi, Amalia Bruni, Paul Fraser, Peter St George-Hyslop

ABSTRACT

Nicastrin, a transmembrane glycoprotein, forms high molecular weight complexes with presenilin 1 and presenilin 2. Suppression of nicastrin expression in Caenorhabditis elegans embryos induces a subset of notch/glp-1 phenotypes similar to those induced by simultaneous null mutations in both presenilin homologues of C. elegans (sel-12 and hop-1). Nicastrin also binds carboxy-terminal derivatives of β-amyloid precursor protein (βAPP), and modulates the production of the amyloid β-peptide (Aβ) from these derivatives. Missense mutations in a conserved hydrophilic domain of nicastrin increase Aβ42 and Aβ40 peptide secretion. Deletions in this domain inhibit Aβ production. Nicastrin and presenilins are therefore likely to be functional components of a multimeric complex necessary for the intramembranous proteolysis of proteins such as Notch/GLP-1 and βAPP. More... »

PAGES

48-54

References to SciGraph publications

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  • Journal

    TITLE

    Nature

    ISSUE

    6800

    VOLUME

    407

    Identifiers

    URI

    http://scigraph.springernature.com/pub.10.1038/35024009

    DOI

    http://dx.doi.org/10.1038/35024009

    DIMENSIONS

    https://app.dimensions.ai/details/publication/pub.1028278722

    PUBMED

    https://www.ncbi.nlm.nih.gov/pubmed/10993067


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