Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Homodimer of two F-box proteins beta TrCP1 or beta TrCP2 binds to I kappa B alpha for signal-dependent ubiquitination
Autore:
Suzuki, H; Chiba, T; Suzuki, T; Fujita, T; Ikenoue, T; Omata, M; Furuichi, K; Shikama, H; Tanaka, K;
Indirizzi:
Japan Sci & Technol Corp, Tokyo Metropolitan Inst Med Sci, Core Res EvolutSci & Technol, Bunkyo Ku, Tokyo 1138613, Japan Japan Sci & Technol Corp Tokyo Japan 1138613 yo Ku, Tokyo 1138613, Japan Yamanouchi Pharmaceut Co Ltd, Inst Drug Discovery Res, Tsukuba, Ibaraki 3058585, Japan Yamanouchi Pharmaceut Co Ltd Tsukuba Ibaraki Japan 3058585 3058585, Japan Univ Tokyo, Fac Med, Dept Gastroenterol, Bunkyo Ku, Tokyo 1138655, Japan Univ Tokyo Tokyo Japan 1138655 oenterol, Bunkyo Ku, Tokyo 1138655, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 4, volume: 275, anno: 2000,
pagine: 2877 - 2884
SICI:
0021-9258(20000128)275:4<2877:HOTFPB>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
SITE-SPECIFIC PHOSPHORYLATION; PROTEASOME PATHWAY; PROTEOLYSIS; DEGRADATION; COMPLEX; ACTIVATION; KINASE; SYSTEM; LIGASE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
47
Recensione:
Indirizzi per estratti:
Indirizzo: Tanaka, K Japan Sci & Technol Corp, Tokyo Metropolitan Inst Med Sci, Core Res EvolutSci & Technol, Bunkyo Ku, 3-18-22 Honkomagome, Tokyo 1138613, Japan Japan Sci & Technol Corp 3-18-22 Honkomagome Tokyo Japan 1138613
Citazione:
H. Suzuki et al., "Homodimer of two F-box proteins beta TrCP1 or beta TrCP2 binds to I kappa B alpha for signal-dependent ubiquitination", J BIOL CHEM, 275(4), 2000, pp. 2877-2884

Abstract

We found previously that overexpression of an F-box protein beta TrCP1 andthe structurally related beta TrCP2 augments ubiquitination of phosphorylated I kappa B alpha (pI kappa B alpha) induced by tumor necrosis factor-alpha (TNF-alpha), but the relationship of the two homologous beta TrCP proteins remains unknown. Herein we reveal that deletion mutants of beta TrCP1 and beta TrCP2 lacking the F-box domain suppressed ubiquitination and destruction of pI kappa B alpha as well as transcriptional activation of NF-kappa B, The ectopically expressed beta TrCP1 and beta TrCP2 formed both homodimer and heterodimer complexes without displaying the trimer complex. Dimerization of beta TrCP1 and/or beta TrCP2 takes place at their conserved NH2-terminal regions, termed a "D-domain" (for dimerization domain), located upstream of the F-box domain. The D-domain was necessary and sufficient for the dimer formation. Intriguingly, the beta TrCP homodimer, but not the heterodimer, was selectively recruited to pI kappa B alpha induced by TNF-alpha. These results indicate that not only beta TrCP1 but also beta TrCP2 participates in the ubiquitination- dependent destruction of I kappa B alpha by forming SCFbeta TrCP1-beta TrCP1 and SCFbeta TrCP2-beta TrCP2 ubiquitin-ligasecomplexes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/03/20 alle ore 17:27:15