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Titolo:
Identification of a novel beta-catenin-interacting protein
Autore:
Kawajiri, A; Itoh, N; Fukata, M; Nakagawa, M; Yamaga, M; Iwamatsu, A; Kaibuchi, K;
Indirizzi:
Nara Inst Sci & Technol, Div Signal Transduct, Ikoma 6300101, Japan Nara Inst Sci & Technol Ikoma Japan 6300101 nsduct, Ikoma 6300101, Japan Nagoya Univ, Sch Med, Dept Cell Pharmacol, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 acol, Nagoya, Aichi 4668550, Japan Kirin Brewery Co Ltd, Cent Labs Key Technol, Yokohama, Kanagawa 2360004, Japan Kirin Brewery Co Ltd Yokohama Kanagawa Japan 2360004 agawa 2360004, Japan
Titolo Testata:
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
fascicolo: 2, volume: 273, anno: 2000,
pagine: 712 - 717
SICI:
0006-291X(20000705)273:2<712:IOANBP>2.0.ZU;2-Q
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CELL ADHESION; SMALL GTPASES; CYTOPLASMIC DOMAIN; MDCK CELLS; S-SCAM; RAP1; CDC42; RAC1; FAMILY; RHO;
Keywords:
beta-catenin; KIAA0313; KIAA0705; Rap1 GEF;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
29
Recensione:
Indirizzi per estratti:
Indirizzo: Kaibuchi, K Nara Inst Sci & Technol, Div Signal Transduct, 8916-5 Takayama, Ikoma 6300101, Japan Nara Inst Sci & Technol 8916-5 Takayama Ikoma Japan6300101 n
Citazione:
A. Kawajiri et al., "Identification of a novel beta-catenin-interacting protein", BIOC BIOP R, 273(2), 2000, pp. 712-717

Abstract

Cadherin is a well-known cell-cell adhesion molecule, and it binds to beta-catenin, which in turn binds to alpha-catenin. However, little is known about the regulatory mechanism underlying the cadherin-mediated cell-cell adhesion. Here we purified two novel beta-catenin-interacting proteins with molecular masses of 180 kDa (p180) and 150 kDa (p150) from bovine brain cytosol by using glutathione S-transferase (GST)-beta-catenin affinity column chromatography. Mass spectral analysis revealed p180 to be identical to KIAA0313 which has a putative Rap1 guanine nucleotide exchange factor (GEF) domain and p150 to be the same as KIAA0705 which has a high degree of sequence similarity to the synaptic scaffolding molecule (S-SCAM), which binds beta-catenin and KIAA0313 in the yeast two-hybrid system and overlay assay, respectively (Ide et al., Biochem. Biophys. Res. Commun. 256, 456-461, 1999; Ohtsuka et al., Biochem. Biophys. Res. Commun. 265, 38-44, 1999). beta-Catenin was coimmunoprecipitated with KIAA0313 in Madin-Darby canine kidney II (MDCKII) cells, bovine brain cytosol, and EL cells. KIAA0313 and beta-cateninwere partly colocalized at sites of cell-cell contact in MDCKII cells. Taken together, our data suggest that KIAA0313 associates with beta-catenin through KIAA0705 in vivo at sites of cell-cell contact. (C) 2000 Academic Press.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/21 alle ore 12:20:08