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Nicastrin modulates presenilin-mediated notch/glp-1 signal transduction and betaAPP processing.

Nature | Sep 7, 2000

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

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.

Pubmed ID: 10993067 RIS Download

Mesh terms: Amino Acid Sequence | Amyloid Precursor Protein Secretases | Amyloid beta-Protein Precursor | Animals | Aspartic Acid Endopeptidases | Caenorhabditis elegans | Caenorhabditis elegans Proteins | DNA, Complementary | Endopeptidases | Humans | Membrane Glycoproteins | Membrane Proteins | Molecular Sequence Data | Presenilin-1 | Presenilin-2 | Receptors, Notch | Sequence Homology, Amino Acid | Signal Transduction | Transfection

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