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Titolo:
Truncated form of importin alpha identified in breast cancer cell inhibitsnuclear import of p53
Autore:
Kim, IS; Kim, DH; Han, SM; Chin, MU; Nam, HJ; Cho, HP; Choi, SY; Song, BJ; Kim, ER; Bae, YS; Moon, YH;
Indirizzi:
Sung Ae Life Sci Res Inst, Kyeonggi 423030, South Korea Sung Ae Life Sci Res Inst Kyeonggi South Korea 423030 23030, South Korea Hannam Univ, Dept Microbiol, Daeduk Gu, Taejon 306791, South Korea Hannam Univ Taejon South Korea 306791 duk Gu, Taejon 306791, South Korea
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 30, volume: 275, anno: 2000,
pagine: 23139 - 23145
SICI:
0021-9258(20000728)275:30<23139:TFOIAI>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
NUCLEOCYTOPLASMIC TRANSPORT; PROTEIN IMPORT; EXPORT SIGNAL; PORE COMPLEX; LOCALIZATION; GENE; MECHANISMS; MUTATIONS; SUBSTRATE; BINDING;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
36
Recensione:
Indirizzi per estratti:
Indirizzo: Moon, YH 389 Chulsan Kwangmyeong, Kyeonggi 423030, South Korea 389 Chulsan Kwangmyeong Kyeonggi South Korea 423030 South Korea
Citazione:
I.S. Kim et al., "Truncated form of importin alpha identified in breast cancer cell inhibitsnuclear import of p53", J BIOL CHEM, 275(30), 2000, pp. 23139-23145

Abstract

Disruption of the function of tumor suppressor proteins occasionally can be dependent on their subcellular localization. In about 40% of the breast cancer tissues, p53 is found in the cytoplasm as opposed to the nucleus, where it resides in normal breast cells. This means that the regulation of subcellular location of p53 is an important mechanism in controlling its function. The transport factors required for the nuclear export of p53 and the mechanisms of their nuclear export have been extensively characterized. However, little is known about the mechanism of nuclear import of p53, p53 contains putative nuclear localization signals (NLSs) which would interact witha nuclear transport factor, importin alpha. In this report we demonstrate that importin a binds to NLSI in p53 and mediates the nuclear import of p53, Reverse transcriptase-polymerase chain reaction and sequencing analyses showed that a truncated importin alpha deleted the region encoding the putative NLS-binding domain of p53, suggesting that it could not bind to NLSs ofp53 proteins. Binding of importin alpha to p53 was confirmed by using yeast two-hybrid assay. When expressed in CHO-K1 cells, the truncated importin alpha predominantly localized to the cytoplasm, In truncated importin alphaexpressing cells, p53 preferentially localized to cytoplasmic sites as well, A significant increase in the p21(waf1/cip1) mRNA level and induction ofapoptosis were also observed in importin alpha overexpressing cells. Theseresults strongly suggest that importin alpha functions as a component of the NLS receptor for p53 and mediates nuclear import of p53.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/12/20 alle ore 20:09:24