Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Promotion of S-Phase entry and cell growth under serum starvation by SAC/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: Association with inhibition of p27 accumulation
Autore:
Duan, HJ; Tsvetkov, LM; Liu, YL; Song, Y; Swaroop, M; Wen, R; Kung, HF; Zhang, H; Sun, Y;
Indirizzi:
Pfizer Global Res & Dev, Dept Biol Mol, Ann Arbor Labs, Ann Arbor, MI 48105 USA Pfizer Global Res & Dev Ann Arbor MI USA 48105 s, Ann Arbor, MI 48105 USA Yale Univ, Sch Med, Dept Genet, New Haven, CT 06510 USA Yale Univ New Haven CT USA 06510 Med, Dept Genet, New Haven, CT 06510 USA NCI, Frederick Canc Res & Dev Ctr, Lab Biochem Physiol, Frederick, MD USA NCI Frederick MD USA s & Dev Ctr, Lab Biochem Physiol, Frederick, MD USA Univ Penn, Sch Med, Dept Ophthalmol & Cell & Dev Biol, Philadelphia, PA 19104 USA Univ Penn Philadelphia PA USA 19104 Dev Biol, Philadelphia, PA 19104 USA
Titolo Testata:
MOLECULAR CARCINOGENESIS
fascicolo: 1, volume: 30, anno: 2001,
pagine: 37 - 46
SICI:
0899-1987(200101)30:1<37:POSEAC>2.0.ZU;2-F
Fonte:
ISI
Lingua:
ENG
Soggetto:
DEPENDENT KINASE INHIBITOR; NF-KAPPA-B; PROTEASOME PATHWAY; CYCLIN UBIQUITINATION; MEDIATED DEGRADATION; CULLIN PARTNERS; CDK INHIBITORS; BREAST-CANCER; P27(KIP1); COMPLEX;
Keywords:
SAC/ROC/Rbx/Hrt; ubiquitin ligase; RING finger; cell growth; serum starvation; p27;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
55
Recensione:
Indirizzi per estratti:
Indirizzo: Sun, Y Pfizer Global Res & Dev, Dept Biol Mol, Ann Arbor Labs, 2800 Plymouth Rd, Ann Arbor, MI 48105 USA Pfizer Global Res & Dev 2800 Plymouth Rd AnnArbor MI USA 48105 USA
Citazione:
H.J. Duan et al., "Promotion of S-Phase entry and cell growth under serum starvation by SAC/ROC2/Rbx2/Hrt2, an E3 ubiquitin ligase component: Association with inhibition of p27 accumulation", MOL CARCINO, 30(1), 2001, pp. 37-46

Abstract

The sensitive-to-apoptosis gene (SAG) was initially identified as a redox-inducible, apoptosis-protective protein and subsequently found to be the second family member of regulator of cullins (ROC)/RING box protein (Rbx)/Hrt, which acts as a component of E3 ubiquitin ligase. We report here that SAGpromoted cell growth under serum starvation. Microinjection of SAC mRNA into quiescent NIH/3T3 cells induced S-phase entry as determined by [H-3]-thymidine incorporation. Likewise, overexpression of SAG by either adenovirus infection of immortalized human epidermal keratinocytes (Rhek-1) or DNA transfection of SY5Y human neuroblastoma cells induced cell proliferation under serum starvation. Because cyclin-dependent kinase inhibitors (CKIs), including p21, p27, and p57, are degraded through the ubiquitin pathway, we tested whether SAG-induced cell growth is associated with CKI degradation. Although there was no significant difference in the levels of p21 and p57 between the Vector controls and SAG-overexpressing cells, serum starvation induced 10- to 18-fold accumulation of p27 in control Rhek-1 cells. Accumulation of p27 was remarkably inhibited (only 2 to 5-fold) in SAG-infected cells. Inhibition of p27 accumulation was also observed in stably SAG-overexpressing SY5Y cells. Significantly, SAG-associated inhibition of p27 accumulation was largely abolished by the treatment with a proteasome inhibitor. In vivo binding of SAG and Skp2, an F-box protein that promotes p27 ubiquitination, was detected, and the binding was enhanced in SAG-overexpressing cells grown under serum starvation. Thus, SAG-induced growth with serum withdrawal appears to be associated with SAG-mediated p27 degradation. (C) 2001 Wiley-Liss, Inc.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 25/01/20 alle ore 16:14:00