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Titolo:
DNA-DAMAGE TRIGGERS DRB-RESISTANT PHOSPHORYLATION OF HUMAN P53 AT THECK2 SITE
Autore:
BLAYDES JP; HUPP TR;
Indirizzi:
UNIV DUNDEE,NINEWELLS HOSP & MED SCH,DEPT MOL & CELLULAR PATHOL DUNDEE DD1 9SY SCOTLAND UNIV DUNDEE,NINEWELLS HOSP & MED SCH,DEPT MOL & CELLULAR PATHOL DUNDEE DD1 9SY SCOTLAND
Titolo Testata:
Oncogene
fascicolo: 8, volume: 17, anno: 1998,
pagine: 1045 - 1052
SICI:
0950-9232(1998)17:8<1045:DTDPOH>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
CASEIN KINASE-II; C-TERMINAL DOMAIN; RNA-POLYMERASE-II; WILD-TYPE P53; TRANSCRIPTIONALLY ACTIVE P53; TUMOR-SUPPRESSOR PROTEIN; CELL-CYCLE ARREST; BINDING ACTIVITY; IN-VITRO; HEAT-SHOCK;
Keywords:
P53; CK2; DRB; UV-IRRADIATION; PHOSPHORYLATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Science Citation Index Expanded
Citazioni:
83
Recensione:
Indirizzi per estratti:
Citazione:
J.P. Blaydes e T.R. Hupp, "DNA-DAMAGE TRIGGERS DRB-RESISTANT PHOSPHORYLATION OF HUMAN P53 AT THECK2 SITE", Oncogene, 17(8), 1998, pp. 1045-1052

Abstract

The sequence-specific DNA binding activity of p53 is negatively regulated by a C-terminal domain whose phosphorylation in vitro can activate the latent DNA binding function of the protein. The DNA binding activity of p53 is a core component of its stress-activated transcription function, yet it is not yet clear whether phosphorylation within the C-terminal domain plays a role in the p53 damage response in vise. As the casein kinase 2 (CK2) site at serine 392 is the C-terminal phosphorylation motif that exhibits the most pronounced conservation at the primary amino acid level, we have focused on determining whether the CK2site is modified in vivo and whether radiation effects the extent of that phosphorylation. Using antibodies that can detect serine 392-phosphorylation of p53, we demonstrate that UV radiation can trigger extensive phosphorylation at the CK2 site. The CK2 inhibitor, 5,6-dichloro-1-beta-D-ribofuranosylbenzimidazole (DRB), can partially inhibit the UV-induced phosphorylation at serine 392, suggesting that CK2 is one ofthe major serine 392-kinases. However, a striking increase in UV-induced serine 392 phosphorylation and p53 transactivation function at higher levels of DRB suggests that a DRB-resistant/stress-activated pathway may target serine 392 irt vivo. These data demonstrate that radiation-induced phosphorylation of p53 can occur in vivo at serine 392 and implicate a CK2-independent signal cascade that can function to modulate serine 392 phosphorylation in cells.

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Documento generato il 21/09/20 alle ore 09:24:13