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Titolo:
Interaction of the hepatitis B virus X protein with the Crm1-dependent nuclear export pathway
Autore:
Forgues, M; Marrogi, AJ; Spillare, EA; Wu, CG; Yang , Q; Yoshida, M; Wang, XW;
Indirizzi:
NCI, Human Carcinogenesis Lab, NIH, Bethesda, MD 20892 USA NCI Bethesda MD USA 20892 Carcinogenesis Lab, NIH, Bethesda, MD 20892 USA Univ Tokyo, Dept Biotechnol, Tokyo, Japan Univ Tokyo Tokyo JapanUniv Tokyo, Dept Biotechnol, Tokyo, Japan
Titolo Testata:
JOURNAL OF BIOLOGICAL CHEMISTRY
fascicolo: 25, volume: 276, anno: 2001,
pagine: 22797 - 22803
SICI:
0021-9258(20010622)276:25<22797:IOTHBV>2.0.ZU;2-H
Fonte:
ISI
Lingua:
ENG
Soggetto:
TATA-BINDING PROTEIN; NF-KAPPA-B; HEPATOCELLULAR-CARCINOMA; MESSENGER-RNA; TRANSACTIVATION FUNCTION; SIGNALING PATHWAY; REV PROTEIN; GENE; DNA; ACTIVATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
52
Recensione:
Indirizzi per estratti:
Indirizzo: Wang, XW NCI, Human Carcinogenesis Lab, NIH, 37 Convent Dr,MSC 4255,Bldg 37,Rm 2C07, Bethesda, MD 20892 USA NCI 37 Convent Dr,MSC 4255,Bldg 37,Rm 2C07 Bethesda MD USA 20892
Citazione:
M. Forgues et al., "Interaction of the hepatitis B virus X protein with the Crm1-dependent nuclear export pathway", J BIOL CHEM, 276(25), 2001, pp. 22797-22803

Abstract

The leucine-rich nuclear export signal (NES) is used to shuttle large cellular proteins from the nucleus to the cytoplasm. The nuclear export receptor Crm1 is essential in this process by recognizing the NES motif. Here, we show that the oncogenic hepatitis B virus (HBV)X protein (HBx) contains a functional NES motif. We found that the predominant cytoplasmic localizationof HBx is sensitive to the drug leptomycin B (LMB), which specifically inactivates Crm1. Mutations at the two con served leucine residues to alanine at the NES motif (L98A,L100A) resulted in a nuclear redistribution of HBx. A recombinant HBx protein binds to Crm1 in vitro. In addition, ectopic expression of HBx sequesters Crm1 in the cytoplasm. Furthermore, HBx activates NF kappaB by inducing its nuclear translocation in a NES-dependent manner. Abnormal cytoplasmic sequestration of Crm1, accompanied by a nuclear localization of NF kappaB, was also observed in hepatocytes from HBV-positive liver samples with chronic active hepatitis. We suggest that Crm1 may play a role in HBx-mediated liver carcinogenesis.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 04/04/20 alle ore 03:01:01