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Titolo:
THE RAS TARGET AF-6 IS A SUBSTRATE OF THE FAM DEUBIQUITINATING ENZYME
Autore:
TAYA S; YAMAMOTO T; KANO K; KAWANO Y; IWAMATSU A; TSUCHIYA T; TANAKA K; KANAIAZUMA M; WOOD SA; MATTICK JS; KAIBUCHI K;
Indirizzi:
NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT,8916-5 TAKAYAMA IKOMA 6300101 JAPAN NARA INST SCI & TECHNOL,DIV SIGNAL TRANSDUCT IKOMA 6300101 JAPAN KIRIN BREWERY CO LTD,CENT LABS KEY TECHNOL,KANAZAWA KU YOKOHAMA KANAGAWA 236000 JAPAN JAPAN SCI & TECHNOL CORP,METROPOLITAN INST MED SCI,CORE RES EVOLUT SCI & TECHNOL,BUNKYO KU TOKYO 1130021 JAPAN UNIV QUEENSLAND,CTR CELLULAR & MOL BIOL ST LUCIA QLD 4072 AUSTRALIA UNIV ADELAIDE,DEPT BIOCHEM ADELAIDE SA 5005 AUSTRALIA
Titolo Testata:
The Journal of cell biology
fascicolo: 4, volume: 142, anno: 1998,
pagine: 1053 - 1062
SICI:
0021-9525(1998)142:4<1053:TRTAIA>2.0.ZU;2-M
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEVELOPING DROSOPHILA EYE; MEDIATED CELL-ADHESION; B-RAF; EPITHELIAL-CELLS; FACETS GENE; SIGNAL-TRANSDUCTION; TIGHT JUNCTIONS; KINASE KINASE; BETA-CATENIN; BOVINE BRAIN;
Keywords:
AF-6; FAM; DEUBIQUITINATING ENZYME; UBIQUITINATION; CELL-CELL ADHESIONS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
47
Recensione:
Indirizzi per estratti:
Citazione:
S. Taya et al., "THE RAS TARGET AF-6 IS A SUBSTRATE OF THE FAM DEUBIQUITINATING ENZYME", The Journal of cell biology, 142(4), 1998, pp. 1053-1062

Abstract

The Ras target AF-6 has been shown to serve as one of the peripheral components of cell-cell adhesions, and is thought to participate in cell-cell adhesion regulation downstream of Ras. We here purified an AF-6-interacting protein with a molecular mass of similar to 220 kD (p220) to investigate the function of AF-6 at cell-cell adhesions. The peptide sequences of p220 were identical to the amino acid sequences of mouse Fam. Fam is homologous to a deubiquitinating enzyme in Drosophila,the product of the fat facets gene. Recent genetic analyses indicate that the deubiquitinating activity of the fnr facets product plays a critical role in controlling the cell fate. We found that Fam accumulated at the cell-cell contact sites of MDCKII cells, but not at free ends of plasma membranes. Fam was partially colocalized with AF-6 and interacted with AF-6 in vivo and in vitro. We also showed that AF-6 was ubiquitinated in intact cells, and that Fam prevented the ubiquitination of AF-6. These results indicate that AF-6 forms a complex with and serves as one of the substrates for Fam, and suggest that the degradation of peripheral components of cell-cell adhesions may be regulated byFam.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 23/01/21 alle ore 02:46:29