Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site
Autore:
Ruffner, H; Jiang, W; Craig, AG; Hunter, T; Verma, IM;
Indirizzi:
Salk Inst Biol Studies, Genet Lab, La Jolla, CA 92037 USA Salk Inst Biol Studies La Jolla CA USA 92037 Lab, La Jolla, CA 92037 USA
Titolo Testata:
MOLECULAR AND CELLULAR BIOLOGY
fascicolo: 7, volume: 19, anno: 1999,
pagine: 4843 - 4854
SICI:
0270-7306(199907)19:7<4843:BIPAS1>2.0.ZU;2-C
Fonte:
ISI
Lingua:
ENG
Soggetto:
SPORADIC BREAST-CANCER; POLYMERASE-II HOLOENZYME; CELL-CYCLE; OVARIAN-CANCER; DNA-DAMAGE; SUBCELLULAR-LOCALIZATION; TRANSCRIPTIONAL ACTIVATION; NUCLEAR PHOSPHOPROTEIN; SUSCEPTIBILITY GENE; CONSERVED DOMAINS;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
82
Recensione:
Indirizzi per estratti:
Indirizzo: Verma, IM Salk037st Biol Studies, Genet Lab, 10010 N Torrey Pines Rd, La Jolla, CA 92 Salk Inst Biol Studies 10010 N Torrey Pines Rd La Jolla CA USA 92037
Citazione:
H. Ruffner et al., "BRCA1 is phosphorylated at serine 1497 in vivo at a cyclin-dependent kinase 2 phosphorylation site", MOL CELL B, 19(7), 1999, pp. 4843-4854

Abstract

BRCA1 is a cell cycle-regulated nuclear protein that is phosphorylated mainly on serine and to a lesser extent on threonine residues. Changes in phosphorylation occur in response to cell cycle progression and DNA damage. Specifically, BRCA1 undergoes hyperphosphorylation during late G(1) and S phases of the cell cycle. Here we report that BRCA1 is phosphorylated in vivo at serine 1497 (S1497), which is part of a cyclin-dependent kinase (CDK) consensus site. S1497 can be phosphorylated in vitro by CDK2-cyclin A or E. BRCA1 coimmunoprecipitates with an endogenous serine threonine protein kinaseactivity that phosphorylates S1497 in vitro. This cellular kinase activityis sensitive to transfection of a dominant negative form of CDK2, as well as the application of the CDK inhibitors p21 and butyrolactone I but not p16. Furthermore, BRCA1 coimmunoprecipitates with CDK2 and cyclin A. These results suggest that the endogenous kinase activity is composed of CDK2-cyclin complexes, at least in part, concordant with the G(1)/S-specific increasein BRCA1 phosphorylation.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 22/01/20 alle ore 09:30:56