CDK9, a member of the CDC2-like family of kinases, binds to GP130, the receptor of the IL-6 family of cytochines (Articolo in rivista)

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  • CDK9, a member of the CDC2-like family of kinases, binds to GP130, the receptor of the IL-6 family of cytochines (Articolo in rivista) (literal)
Anno
  • 2002-01-01T00:00:00+01:00 (literal)
Alternative label
  • Falco GD.1-2, Neri LM.3-4, Falco MD.5, Bellan C.1-2, Yu Z.6, Luca AD.7, Leoncini L.1, Giordano A.1 (2002)
    CDK9, a member of the CDC2-like family of kinases, binds to GP130, the receptor of the IL-6 family of cytochines
    in Oncogene (Basingstoke)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Falco GD.1-2, Neri LM.3-4, Falco MD.5, Bellan C.1-2, Yu Z.6, Luca AD.7, Leoncini L.1, Giordano A.1 (literal)
Pagina inizio
  • 7464 (literal)
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  • 7470 (literal)
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  • Lavoro multidisciplinare in collaborazione internazionale I.F. 6,737 (literal)
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  • 21 (literal)
Rivista
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  • I.F. 6,737 (literal)
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  • Cdk9 is a member of the Cdc2-like family of kinases. It binds to members of the family of cyclin T (T1, T2a and T2b) and to cyclin K. The Cdk9/cyclin T complex appears to be involved in regulating several physiological processes. Here we show that Cdk9 interacts with gp130, the receptor of the Interleukin-6 (IL-6) family of cytokines, which includes Leukemia Inhibitory Factor (LIF), Oncostatin M (OSM), Ciliary Neurotrophic Factor (CNTF), Interleukin-11 (IL-11) and Cardiotrophin (CT-1). IL-6 is a key regulator of hematopoiesis, immunological responses and inflammation. In addition, IL-6 plays a major role in the endocrine and nervous systems. Signal transduction by gp130 is mediated by physical interaction of the cytoplasmic region of gp130 with cellular kinases and results in the transcriptional activation of cellular and viral genes. We found that Cdk9 interacts in vitro with the cytoplasmic region of gp130 and we succeded in reproducing this interaction in vivo. Cdk9 expression was found both in the nucleus and in the cytoplasm. The binding occurring between Cdk9 and gp130 increased upon IL-6 stimulation. We also observed that Cdk9 synergized with IL-6 in inducing the activation of an IL-6-responsive reporter plasmid. In summary, these results point to a previously undisclosed role for Cdk9 in signal transduction (literal)
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  • ISI Web of Science (WOS) (literal)
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  • 1Sbarro Institute for Cancer Research & Molecular Medicine, Temple University, Philadelphia, USA 2Istituto di Anatomia e Istologia Patologica, Uni. Siena 3Dipartimento di Morfologia ed Embriologia, Sezione di Anatomia Umana, Uni. Ferrara 4Istituto di Citomorfologia Normale e Patologica - CNR 5Dipartimento di Biologia Evolutiva e Comparata, Uni. Federico II di Napoli 6Jefferson Medical College, Philadelphia, USA 7Istituto di Anatomia Topografica, Seconda Uni. Napoli (literal)
Titolo
  • CDK9, a member of the CDC2-like family of kinases, binds to GP130, the receptor of the IL-6 family of cytochines (literal)
Abstract
  • Cdk9 is a member of the Cdc2-like family of kinases. It binds to members of the family of cyclin T (T1, T2a and T2b) and to cyclin K. The Cdk9/cyclin T complex appears to be involved in regulating several physiological processes. In fact Cdk9 is the kinase of the P-TEFb complex, involved in basal transcription. Cdk9 has also been described as the kinase of the TAK complex, homologous to P-TEFb and involved in HIV replication. Here we show that Cdk9 interacts with gp130, the receptor of the Interleukin-6 (IL-6) family of cytokines, which includes Leukemia Inhibitory Factor (LIF), Oncostatin M (OSM), Ciliary Neurotrophic Factor (CNTF), Interleukin-11 (IL-11) and Cardiotrophin (CT-1). IL-6 is a key regulator of hematopoiesis, immunological responses and inflammation. In addition, IL-6 plays a major role in the endocrine and nervous systems. Signal transduction by gp130 is mediated by physical interaction of the cytoplasmic region of gp130 with cellular kinases and results in the transcriptional activation of cellular and viral genes. We found that Cdk9 interacts in vitro with the cytoplasmic region of gp130 and we succeded in reproducing this interaction in vivo. Cdk9 expression was found both in the nucleus and in the cytoplasm. The binding occurring between Cdk9 and gp130 increased upon IL-6 stimulation. We also observed that Cdk9 synergized with IL-6 in inducing the activation of an IL-6-responsive reporter plasmid. In summary, these results point to a previously undisclosed role for Cdk9 in signal transduction. (literal)
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