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Titolo:
Domains of Axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization
Autore:
Fagotto, F; Jho, EH; Zeng, L; Kurth, T; Joos, T; Kaufmann, C; Costantini, F;
Indirizzi:
Columbia Univ Coll Phys & Surg, Dept Genet & Dev, New York, NY 10032 USA Columbia Univ Coll Phys & Surg New York NY USA 10032 w York, NY 10032 USA Max Planck Inst Dev Biol, Div Cell Biol, D-72076 Tubingen, Germany Max Planck Inst Dev Biol Tubingen Germany D-72076 2076 Tubingen, Germany
Titolo Testata:
JOURNAL OF CELL BIOLOGY
fascicolo: 4, volume: 145, anno: 1999,
pagine: 741 - 756
SICI:
0021-9525(19990517)145:4<741:DOAIIP>2.0.ZU;2-5
Fonte:
ISI
Lingua:
ENG
Soggetto:
ADENOMATOUS POLYPOSIS-COLI; TUMOR-SUPPRESSOR PROTEIN; GLYCOGEN-SYNTHASE KINASE-3; XENOPUS-LAEVIS EMBRYOS; MOUSE FUSED LOCUS; BETA-CATENIN; SIGNALING PATHWAY; NEGATIVE REGULATOR; APC GENE; WINGLESS;
Keywords:
beta-catenin; glycogen synthase kinase 3 beta (GSK3 beta) adenomatous polyposis coli (APC); Dishevelled (Dsh); dorsal axis formation;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Costantini, F Columbia Univ Coll Phys & Surg, Dept Genet & Dev, 701 W 168th St, New York, Columbia Univ Coll Phys & Surg 701 W 168th St New York NY USA 10032
Citazione:
F. Fagotto et al., "Domains of Axin involved in protein-protein interactions, Wnt pathway inhibition, and intracellular localization", J CELL BIOL, 145(4), 1999, pp. 741-756

Abstract

Axin was identified as a regulator of embryonic axis induction in vertebrates that inhibits the Wnt signal transduction pathway. Epistasis experiments in frog embryos indicated that Axin functioned downstream of glycogen synthase kinase 3 beta (GSK3 beta) and upstream of beta-catenin, and subsequent studies showed that Axin is part of a complex including these two proteins and adenomatous polyposis coli (APC). Here, we examine the role of different Axin domains in the effects on axis formation and beta-catenin levels. We find that the regulators of G-protein signaling domain (major APC-binding site) and GSK3 beta-binding site are required, whereas the COOH-terminal sequences, including a protein phosphatase 2A binding site and the DIX domain, are not essential, Some forms of Axin lacking the beta-catenin binding site can still interact indirectly with beta-catenin and regulate beta-catenin levels and axis formation. Thus in normal embryonic cells, interaction with APC and GSK3 beta is critical for the ability of Axin to regulate signaling via beta-catenin. Myc-tagged Axin is localized in a characteristic pattern of intracellular spots as well as at the plasma membrane. NH2-terminal sequences were required for targeting to either of these sites, whereas COOH-terminal sequences increased localization at the spots. Coexpression ofhemagglutinin-tagged Dishevelled (Dsh) revealed strong colocalization withAxin, suggesting that Dsh can interact with the Axin/APC/GSK3/beta-catenincomplex, and may thus modulate its activity.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 05/07/20 alle ore 13:37:51