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Titolo:
Identification of major phosphorylation sites of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP): Ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylation
Autore:
Yokoyama, A; Tanaka, M; Matsuda, G; Kato, K; Kanamori, M; Kawasaki, H; Hirano, H; Kitabayashi, I; Ohki, M; Hirai, K; Kawaguchi, Y;
Indirizzi:
Tokyo Med & Dent Univ, Med Res Inst, Dept Tumor Virol, Div Virol Immunol,Bunkyo Ku, Tokyo 1138510, Japan Tokyo Med & Dent Univ Tokyo Japan 1138510 unkyo Ku, Tokyo 1138510, Japan Yokohama City Univ, Kihara Inst Biol Res, Div Plant Engn, Yokohama, Kanagawa 244, Japan Yokohama City Univ Yokohama Kanagawa Japan 244 ohama, Kanagawa 244, Japan Natl Canc Ctr, Res Inst, Canc Genom Div, Chuo Ku, Tokyo 1040045, Japan Natl Canc Ctr Tokyo Japan 1040045 nom Div, Chuo Ku, Tokyo 1040045, Japan
Titolo Testata:
JOURNAL OF VIROLOGY
fascicolo: 11, volume: 75, anno: 2001,
pagine: 5119 - 5128
SICI:
0022-538X(200106)75:11<5119:IOMPSO>2.0.ZU;2-J
Fonte:
ISI
Lingua:
ENG
Soggetto:
HISTONE ACETYLATION; IN-VITRO; KINASE; TRANSCRIPTION; LOCALIZATION; EXPRESSION; GENE; IMMORTALIZATION; RETINOBLASTOMA; TRANSFECTION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
43
Recensione:
Indirizzi per estratti:
Indirizzo: Kawaguchi, Y Tokyo Med & Dent Univ, Med Res Inst, Dept Tumor Virol, Div Virol Immunol,Bunkyo Ku, Tokyo 1138510, Japan Tokyo Med & Dent Univ Tokyo Japan 1138510 yo 1138510, Japan
Citazione:
A. Yokoyama et al., "Identification of major phosphorylation sites of Epstein-Barr virus nuclear antigen leader protein (EBNA-LP): Ability of EBNA-LP to induce latent membrane protein 1 cooperatively with EBNA-2 is regulated by phosphorylation", J VIROLOGY, 75(11), 2001, pp. 5119-5128

Abstract

Epstein-Barr virus (EBV) nuclear antigen leader protein (EBNA-LP) is a phosphoprotein suggested to play important roles in EBV-induced immortalization of B cells. One of the potential functions of EBNA-LP is a cooperative induction with EBNA-2 of viral and cellular gene expression, including that of the genes for viral latent membrane protein 1 (LMP-1) and cellular cyclinD2. We report here that the phosphorylation of EBNA-LP by cellular kinase(s) is critical to its ability to cooperate with EBNA-2 in up-regulating theexpression of LMP-1 in a B-lymphoma cell line. Our conclusion is based on the following observations. (i) Mass-spectrometric analysis of purified EBNA-LP and mutational analyses of EBNA-LP revealed that the serine residue atposition 35 in the W2 repeat domain is the major phosphorylation site of EBNA-LP in vivo. (ii) Substitutions of this site in each W2 repeat domain with alanine markedly reduced the ability of the protein to induce LMP-1 expression in combination with EBNA-2 in Akata cells. (iii) Replacement at the major phosphorylation sites with glutamic acids restored the wild-type phenotype. It is well established that this substitution mimics constitutive phosphorylation. These results indicated that the coactivator function of EBNA-LP is regulated by phosphorylation.

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Documento generato il 07/07/20 alle ore 15:05:19