Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A mode of regulation of beta-catenin signaling activity in Xenopus embryosindependent of its levels
Autore:
Guger, KA; Gumbiner, BM;
Indirizzi:
Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, New York, NY 10021 USA Mem Sloan Kettering Canc Ctr New York NY USA 10021 New York, NY 10021 USA
Titolo Testata:
DEVELOPMENTAL BIOLOGY
fascicolo: 2, volume: 223, anno: 2000,
pagine: 441 - 448
SICI:
0012-1606(20000715)223:2<441:AMOROB>2.0.ZU;2-W
Fonte:
ISI
Lingua:
ENG
Soggetto:
GLYCOGEN-SYNTHASE KINASE-3; MOLECULE E-CADHERIN; TRANSCRIPTIONAL ACTIVATION; NUCLEAR-LOCALIZATION; PATHWAY; ARMADILLO; PROTEIN; AXIS; EXPRESSION; DROSOPHILA;
Keywords:
signal transduction; GSK3 beta; Wnts; Xenopus;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
35
Recensione:
Indirizzi per estratti:
Indirizzo: Gumbiner, BM Mem Sloan Kettering Canc Ctr, Cellular Biochem & Biophys Program, Box 564,1275 York Ave, New York, NY 10021 USA Mem Sloan Kettering CancCtr Box 564,1275 York Ave New York NY USA 10021
Citazione:
K.A. Guger e B.M. Gumbiner, "A mode of regulation of beta-catenin signaling activity in Xenopus embryosindependent of its levels", DEVELOP BIO, 223(2), 2000, pp. 441-448

Abstract

The signaling activity of beta-catenin is thought to be regulated by phosphorylation of a cluster of N-terminal serines, putative sites for GSK3 beta. In the prevailing model in the literature, GSK3 beta-dependent phosphorylation of these sites targets beta-catenin for ubiquitin-mediated degradation. Wnt signaling inhibits GSK3 beta activity and this blocks degradation, allowing beta-catenin to accumulate and signal. We show here that beta-catenin activity is not regulated solely by protein stability. Mutations in the putative GSK3 beta phosphorylation sites of beta-catenin enhance its signaling activity, but this cannot be accounted for by accumulation of either total or cadherin-free protein. Instead, the mutant protein has a threefold higher specific activity than the wild type both in vivo and in an in vitro signaling assay. We conclude that the N-terminal serines convey a layer of regulation upon beta-catenin signaling in addition to the effects these sites exert upon protein stability. (C) 2000 Academic Press

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/07/20 alle ore 22:21:22