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Titolo:
Nicastrin binds to membrane tethered Notch
Autore:
Chen, FS; Yu, G; Arawaka, S; Nishimura, M; Kawarai, T; Yu, H; Tandon, A; Supala, A; Song, YQ; Rogaeva, E; Milman, P; Sato, C; Yu, C; Janus, C; Lee, J; Song, LX; Zhang, LL; Fraser, PE; St George-Hyslop, PH;
Indirizzi:
Univ Toronto, Ctr Res Neurodegenerat Dis, Toronto, ON M5S 3H2, Canada UnivToronto Toronto ON Canada M5S 3H2 t Dis, Toronto, ON M5S 3H2, Canada Univ Toronto, Dept Med Biophys, Toronto, ON M5S 3H2, Canada Univ Toronto Toronto ON Canada M5S 3H2 ophys, Toronto, ON M5S 3H2, Canada Univ Toronto, Dept Med, Toronto, ON M5S 3H2, Canada Univ Toronto Toronto ON Canada M5S 3H2 t Med, Toronto, ON M5S 3H2, Canada Shiga Univ Med Sci, Mol Neurosci Res Ctr, Shiga 5202192, Japan Shiga Univ Med Sci Shiga Japan 5202192 sci Res Ctr, Shiga 5202192, Japan Schering Plough Corp, Res Inst, Dept CNS & Cardiovsc Res, Kenilworth, NJ 07033 USA Schering Plough Corp Kenilworth NJ USA 07033 es, Kenilworth, NJ 07033 USA Toronto Western Hosp, Univ Hlth Network, Dept Med Neurol, Toronto, ON M5T 2S8, Canada Toronto Western Hosp Toronto ON Canada M5T 2S8 oronto, ON M5T 2S8, Canada
Titolo Testata:
NATURE CELL BIOLOGY
fascicolo: 8, volume: 3, anno: 2001,
pagine: 751 - 754
SICI:
1465-7392(200108)3:8<751:NBTMTN>2.0.ZU;2-4
Fonte:
ISI
Lingua:
ENG
Soggetto:
AMYLOID PRECURSOR PROTEIN; FAMILIAL ALZHEIMERS-DISEASE; GAMMA-SECRETASE; INTRACELLULAR DOMAIN; MISSENSE MUTATIONS; MAMMALIAN-CELLS; PRESENILIN; GENE; ENDOPROTEOLYSIS; DROSOPHILA;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
30
Recensione:
Indirizzi per estratti:
Indirizzo: St George-Hyslop, PH Univ Toronto, Ctr Res Neurodegenerat Dis, Tanz Neurosci Bldg,6 Queens Pk Crescent W, Toronto, ON M5S 3H2, Canada Univ Toronto Tanz Neurosci Bldg,6 Queens Pk Crescent W Toronto ON Canada M5S 3H2
Citazione:
F.S. Chen et al., "Nicastrin binds to membrane tethered Notch", NAT CELL BI, 3(8), 2001, pp. 751-754

Abstract

The presenilins(1,2) and nicastrin(3), a type 1 transmembrane glycoprotein, form high molecular weight complexes that are involved in cleaving the beta -amyloid precursor protein (beta APP)(3-7) and Notch(8-11) in their transmembrane domains. The former process (termed gamma -secretase cleavage) generates amyloid beta -peptide (A beta), which is involved in the pathogenesis of Alzheimer's disease. The latter process (termed S3-site cleavage) generates Notch intracellular domain (NICD), which is involved in intercellular signalling. Nicastrin binds both full-length beta APP and the substrates of gamma -secretase (C99- and C83-beta APP fragments), and modulates the activity of gamma -secretase. Although absence of the Caenorhabditis elegans nicastrin homologue (aph-2) is known to cause an embryonic-lethal glp-1 phenotype(3,12), the role of nicastrin in this process has not been explored. Here we report that nicastrin binds to membrane-tethered forms of Notch (substrates for S3-site cleavage of Notch), and that, although mutations in the conserved 312-369 domain of nicastrin strongly modulate gamma -secretase,they only weakly modulate the S3-site cleavage of Notch. Thus, nicastrin has a similar role in processing Notch and beta APP, but the 312-369 domain may have differential effects on these activities. In addition, we report that the Notch and beta APP pathways do not significantly compete with each other.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 18/01/20 alle ore 21:29:58