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Titolo:
RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins
Autore:
Laj, A; Lee, JM; Yang, WM; DeCaprio, JA; Kaelin, WG; Seto, E; Branton, PE;
Indirizzi:
McGill Univ, Dept Biochem, Montreal, PQ H3G 1Y6, Canada McGill Univ Montreal PQ Canada H3G 1Y6 chem, Montreal, PQ H3G 1Y6, Canada McGill Univ, Dept Oncol, Montreal, PQ H3G 1Y6, Canada McGill Univ Montreal PQ Canada H3G 1Y6 ncol, Montreal, PQ H3G 1Y6, Canada Univ S Florida, Mol Oncol Program, H Lee Moffitt Canc Ctr & Res Inst, Tampa, FL 33612 USA Univ S Florida Tampa FL USA 33612 anc Ctr & Res Inst, Tampa, FL 33612 USA Dana Farber Canc Inst, Boston, MA 02115 USA Dana Farber Canc Inst Boston MA USA 02115 Canc Inst, Boston, MA 02115 USA Harvard Univ, Sch Med, Boston, MA 02115 USA Harvard Univ Boston MA USA 02115 vard Univ, Sch Med, Boston, MA 02115 USA Howard Hughes Med Inst, Boston, MA 02115 USA Howard Hughes Med Inst Boston MA USA 02115 Med Inst, Boston, MA 02115 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 10, volume: 19, anno: 1999,
pagine: 6632 - 6641
SICI:
0270-7306(199910)19:10<6632:RRBHDA>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
CELL-CYCLE ARREST; TRANSCRIPTIONAL REPRESSION; ADENOVIRUS E1A; GENE-PRODUCT; DOMAIN; BINDING; E2F1; ACETYLATION; PROMOTER; CLONING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
49
Recensione:
Indirizzi per estratti:
Indirizzo: Branton, PE McGill Univ, Dept Biochem, McIntyre Med Bldg,3655 Drummond St,Montreal, PQ H3G 1Y6, Canada McGill Univ McIntyre Med Bldg,3655 Drummond St Montreal PQ Canada H3G 1Y6
Citazione:
A. Laj et al., "RBP1 recruits both histone deacetylase-dependent and -independent repression activities to retinoblastoma family proteins", MOL CELL B, 19(10), 1999, pp. 6632-6641

Abstract

Retinoblastoma (RB) tumor suppressor family proteins block cell proliferation in part by repressing certain E2F-specific promoters, Both histone deacetylase (HDAC)-dependent and -independent repression activities are associated with the RE "pocket. " The mechanism by which these two repression functions occupy the pocket is unknown. A known RE-binding protein, RBP1, was previously found by our group to be an active corepressor which, if overexpressed, represses E2F-mediated transcription via its association with the pocket. We show here that RBP1 contains two repression domains, one of which binds all three known HDACs and represses them in an HDAC-dependent manner while the other domain functions independently of the HDACs. Thus, RE familymembers repress transcription by recruiting RBP1 to the pocket. RBP1, in turn, serves as a bridging molecule to recruit HDACs and, in addition, provides a second HDAC-independent repression function.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 06/04/20 alle ore 02:10:15