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Titolo:
The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappa B-dependent expression of antiapoptotic factors
Autore:
Akari, H; Bour, S; Kao, S; Adachi, A; Strebel, K;
Indirizzi:
NIAID, Mol Microbiol Lab, NIH, Bethesda, MD 20892 USA NIAID Bethesda MD USA 20892 ol Microbiol Lab, NIH, Bethesda, MD 20892 USA Univ Tokushima, Sch Med, Dept Virol, Tokushima 7708503, Japan Univ Tokushima Tokushima Japan 7708503 t Virol, Tokushima 7708503, Japan
Titolo Testata:
JOURNAL OF EXPERIMENTAL MEDICINE
fascicolo: 9, volume: 194, anno: 2001,
pagine: 1299 - 1311
SICI:
0022-1007(20011105)194:9<1299:THIVT1>2.0.ZU;2-0
Fonte:
ISI
Lingua:
ENG
Soggetto:
INDUCED CELL-DEATH; PLASMA-MEMBRANE; T-CELLS; PARTICLE RELEASE; CYTOCHROME-C; TRANSCRIPTION FACTORS; TRANSMEMBRANE DOMAIN; CYTOPLASMIC DOMAIN; CASPASE ACTIVATION; HIV-1 INFECTION;
Keywords:
TrCP; caspase; TNF-alpha; Bcl-xL; TRAF1;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
77
Recensione:
Indirizzi per estratti:
Indirizzo: Strebel, K NIAID, Mol Microbiol Lab, NIH, 4-312 4 Ctr Dr,MSC 0460, Bethesda, MD 20892USA NIAID 4-312 4 Ctr Dr,MSC 0460 Bethesda MD USA 20892 MD 20892USA
Citazione:
H. Akari et al., "The human immunodeficiency virus type 1 accessory protein Vpu induces apoptosis by suppressing the nuclear factor kappa B-dependent expression of antiapoptotic factors", J EXP MED, 194(9), 2001, pp. 1299-1311

Abstract

Human immunodeficiency virus (HIV) type 1 Vpu is an integral membrane protein with a unique affinity for beta TrCP (TrCP), a key member of the SkpI-Cullin-F-box E3 ubiquitin ligase complex that is involved in the regulated degradation of cellular proteins, including I kappaB. Remarkably, Vpu is resistant to TrCP-mediated degradation and competitively inhibits TrCP-dependent degradation of I kappaB, resulting in the suppression of nuclear factor (NF)-kappaB activity in Vpu-expressing cells. We now report that Vpu, through its interaction with TrCP, potently contributes to the induction of apoptosis in HIV-infected T cells. Vpu-induced apoptosis is specific and independent of other viral proteins. Mutation of a TrCP-binding motif in Vpu abolishes its apoptogenic property, demonstrating a close correlation between this property of Vpu and its ability to inhibit NF-kappaB activity. The involvement of NF-kappaB in Vpu-induced apoptosis is further supported by the finding that the levels of antiapoptotic factors Bcl-xL, A1/Bfl-1, and TNF receptor-associated factor (TRAF)1, all of which are expressed in an NF-kappaB-dependent manner, are reduced and, at the same time, levels of active caspase-3 are elevated. Thus, Vpu induces apoptosis through activation of thecaspase pathway by way of inhibiting the NF-kappaB-dependent expression ofantiapoptotic genes.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/12/20 alle ore 15:24:30