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Titolo:
A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob
Autore:
Suzuki, T; Matsuda, S; Tsuzuku, JK; Yoshida, Y; Yamamoto, T;
Indirizzi:
Univ Tokyo, Inst Med Sci, Dept Oncol, Minato Ku, Tokyo 1088639, Japan UnivTokyo Tokyo Japan 1088639 pt Oncol, Minato Ku, Tokyo 1088639, Japan Nagoya Univ, Sch Med, Dept Mol Pathogenesis, Showa Ku, Nagoya, Aichi 4668550, Japan Nagoya Univ Nagoya Aichi Japan 4668550 a Ku, Nagoya, Aichi 4668550, Japan
Titolo Testata:
GENES TO CELLS
fascicolo: 2, volume: 6, anno: 2001,
pagine: 131 - 138
SICI:
1356-9597(200102)6:2<131:ASKPPT>2.0.ZU;2-R
Fonte:
ISI
Lingua:
ENG
Soggetto:
TRANSCRIPTIONAL REGULATORY COMPLEX; RIBOSOMAL S6 KINASE; KAPPA-B-ALPHA; TOB/BTG1 FAMILY; GROWTH-FACTOR; GENE; EXPRESSION; COMPONENT; CLONING; DOMAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
27
Recensione:
Indirizzi per estratti:
Indirizzo: Yamamoto, T Univ Tokyo, Inst Med Sci, Dept Oncol, Minato Ku, 4-6-1 Shirokanedai, Tokyo1088639, Japan Univ Tokyo 4-6-1 Shirokanedai Tokyo Japan 1088639 8639, Japan
Citazione:
T. Suzuki et al., "A serine/threonine kinase p90rsk1 phosphorylates the anti-proliferative protein Tob", GENES CELLS, 6(2), 2001, pp. 131-138

Abstract

Background: tob is a member of a gene family with antiproliferative function. Over-expression of Tob in NIH3T3 cells results in the suppression of cell. proliferation. The growth suppression is hampered by the presence of activated ErbB2 kinase. The molecular mechanisms by which Tob suppresses cellgrowth and by which ErbB2 abrogates Tob function remain to be elucidated. Results: We show that Tob is phosphorylated on serines and threonines, butnot tyrosines, by a kinase(s) that associates with Tob in the lysates of various cells, including ErbB2-over-expressed cells. We also show that a 95 kDa kinase associates with Tob in vitro. The autophosphorylation activity of this kinase co-chromatographes with Tob-phosphorylating activity, suggesting that the 95 kDa kinase phosphorylates Tob. Among the known kinases withmolecular mass around 95 kDa, p90rsk1 associates with Tob in vitro and in vivo, and phosphorylates Tob at least in vitro. Therefore, it is likely that p90rsk1 represents the 95 kDa kinase and is involved in the regulation ofTob function through phosphorylation. Conclusion: p90rsk1 associates with and phosphorylates Tob. Because p90rsk1 is activated downstream of receptor tyrosine kinases, we propose that Tobfunction is at least in part under the control of growth factor-stimulatedtyrosine kinases through its phosphorylation by p90rsk1.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 27/01/20 alle ore 01:39:18