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Titolo:
Accumulation of soluble and nucleolar-associated p53 proteins following cellular stress
Autore:
Klibanov, SA; OHagan, HM; Ljungman, M;
Indirizzi:
Univ Michigan, Ctr Comprehens Canc, Dept Radiat Oncol, Div Canc Biol, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 v Canc Biol, Ann Arbor, MI 48109 USA Univ Michigan, Sch Med, Mol & Cellular Biol Program, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 iol Program, Ann Arbor, MI 48109 USA
Titolo Testata:
JOURNAL OF CELL SCIENCE
fascicolo: 10, volume: 114, anno: 2001,
pagine: 1867 - 1873
SICI:
0021-9533(200105)114:10<1867:AOSANP>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
RING-FINGER DOMAIN; RNA-POLYMERASE-II; DNA-DAMAGE; PROTEASOME INHIBITORS; UV-RADIATION; MOUSE CELLS; IN-VIVO; MDM2; PHOSPHORYLATION; EXPRESSION;
Keywords:
UV light; proteasome inhibitors; transcription; nucleolus; MDM2;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
51
Recensione:
Indirizzi per estratti:
Indirizzo: Ljungman, M Univ Michigan, Ctr Comprehens Canc, Dept Radiat Oncol, Div Canc Biol, Ann Arbor, MI 48109 USA Univ Michigan Ann Arbor MI USA 48109 Ann Arbor, MI 48109 USA
Citazione:
S.A. Klibanov et al., "Accumulation of soluble and nucleolar-associated p53 proteins following cellular stress", J CELL SCI, 114(10), 2001, pp. 1867-1873

Abstract

The tumor suppressor p53 is a nucleocytoplasmic shuttling protein that accumulates in the nucleus of cells exposed to various cellular stresses. One important role of nuclear p53 is to mobilize a stress response by transactivating target genes such as the p21(Waf1) gene. In this study, we investigated more closely the localization of p53 in cells following various stresses. Immunocytochemistry of fixed human fibroblasts treated with either UV light, the kinase and transcription inhibitor DRB or the proteasome inhibitorMG132 revealed abundant p53 localized to the nucleus. When cells treated with UV or DRB were permeabilized prior to fixation to allow soluble proteins to diffuse, the nuclear p53 signal was abolished. However, in cells treated with MG132, residual p53 localized to distinct large foci, Furthermore, nucleolin co-localized with p53 to these foci, suggesting that these foci were nucleolar structures. Interestingly, the MDM2 protein was found to co-localize with p53 to nucleolar structures following proteasome inhibition. Our results suggest that the p53 proteins accumulating in the nucleus following UV-irradiation or blockage of transcription are freely soluble and, thus, should be able to roam the nucleus to ensure high occupancy of p53 binding sites. However, inhibition of proteasome activity may be a unique stressin that it leads to the sequestering of p53 proteins to the nucleolus, thereby blunting the p53-mediated transactivation of target genes.

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Documento generato il 30/11/20 alle ore 07:06:26