Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the A alpha subunit gene
Autore:
Ruediger, R; Pham, HT; Walter, G;
Indirizzi:
Univ Calif San Diego, Dept Pathol, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 Pathol, La Jolla, CA 92093 USA
Titolo Testata:
ONCOGENE
fascicolo: 1, volume: 20, anno: 2001,
pagine: 10 - 15
SICI:
0950-9232(20010104)20:1<10:DOPP2S>2.0.ZU;2-K
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE THREONINE PHOSPHATASES; REGULATORY B-SUBUNITS; PP2A CORE ENZYME; MOLECULAR-CLONING; CATALYTIC SUBUNIT; SEQUENCE-ANALYSIS; TUMOR-ANTIGENS; OKADAIC ACID; PPP2R1B GENE; T-ANTIGENS;
Keywords:
PP2A; A alpha subunit; mutation; human cancer; tumor suppressor;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
45
Recensione:
Indirizzi per estratti:
Indirizzo: Walter, G Univ Calif San Diego, Dept Pathol, La Jolla, CA 92093 USA Univ Calif San Diego La Jolla CA USA 92093 Jolla, CA 92093 USA
Citazione:
R. Ruediger et al., "Disruption of protein phosphatase 2A subunit interaction in human cancers with mutations in the A alpha subunit gene", ONCOGENE, 20(1), 2001, pp. 10-15

Abstract

The A subunit of protein phosphatase 2A (PP2A) consists of 15 nonidenticalrepeats. The catalytic C subunit binds to C-terminal repeats 11-15 and regulatory B subunits bind to N-terminal repeats 1-10, Recently, four cancer-associated mutants of the A alpha subunit have been described: Glu64-->Asp in lung carcinoma, Glu64 --> Gly in breast carcinoma, Arg418 --> Trp in melanoma, and Delta 171-589 in breast carcinoma, Based on our model of PP2A, wepredicted that Glu64-->Asp and Glu64-->Gly might be defective in B subunitbinding, whereas Arg418-->Trp and Delta 171 - 589 might bind neither B norC subunits, We generated these mutants by site-directed mutagenesis and assayed their ability to associate with different forms of B subunits (B, B',B") or with the catalytic C subunit, The results demonstrate that all mutants are defective in binding either B or B and C subunits, Specifically, the N-terminal mutants, Glu64-->Asp and Glu64-->Gly, are defective in B' but normal in B, B", and C subunit binding, whereas the C-terminal mutants Arg418-->Trp and Delta 171-589 bind none of the B subunits nor the C subunit, The implications of these findings with regard to the potential role of PP2Aas a tumor suppressor are discussed.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 01:44:52