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25 April 2024

» pubmed » pmid10993067

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Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing
G Yu ; M Nishimura ; S Arawaka ; D Levitan ; L Zhang ; A Tandon ; Y Q Song ; E Rogaeva ; F Chen ; T Kawarai ; A Supala ; L Levesque ; H Yu ; D S Yang ; E Holmes ; P Milman ; Y Liang ; D M Zhang ; D H Xu ; C Sato ; E Rogaev ; M Smith ; C Janus ; Y Zhang ; R Aebersold ; L S Farrer ; S Sorbi ; A Bruni ; P Fraser ; P St George-Hyslop ;
Date:	7 Sep 2000
Journal:	Nature, 407 (6800), 48-54
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 beta-amyloid precursor protein (betaAPP), and modulates the production of the amyloid beta-peptide (A beta) from these derivatives. Missense mutations in a conserved hydrophilic domain of nicastrin increase A beta42 and A beta40 peptide secretion. Deletions in this domain inhibit A beta 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 betaAPP.
Source:	PubMed, pmid10993067 doi: 10.1038/35024009
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