Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon a/b and for signal trasduction. (Articolo in rivista)

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  • Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon a/b and for signal trasduction. (Articolo in rivista) (literal)
Anno
  • 1995-01-01T00:00:00+01:00 (literal)
Alternative label
  • Laura Velazquez, Knud E. Mogensen (1), Giovanna Barbieri, Marc Fellous, Gilles Uzé (1) and Sandra Pellegrini. (1995)
    Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon a/b and for signal trasduction.
    in The Journal of biological chemistry (Print); American society for biochemistry and molecular biology, Baltimore (Stati Uniti d'America)
    (literal)
Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
  • Laura Velazquez, Knud E. Mogensen (1), Giovanna Barbieri, Marc Fellous, Gilles Uzé (1) and Sandra Pellegrini. (literal)
Pagina inizio
  • 3327 (literal)
Pagina fine
  • 3334 (literal)
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  • 270 (literal)
Rivista
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  • 8 (literal)
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  • 7 (literal)
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  • Institut Pasteur, INSERM U 276, Paris 75724 Cedex 15, France, (1) Institut de Génétique Moléculaire, CNRS UMR 9942, Montpellier, France. (literal)
Titolo
  • Distinct domains of the protein tyrosine kinase tyk2 required for binding of interferon a/b and for signal trasduction. (literal)
Abstract
  • tyk2 belongs to the JAK family of nonreceptor protein tyrosine kinases recently found implicated in signaling through a large number of cytokine receptors. These proteins are characterized by a large amino-terminal region and two tandemly arranged kinase domains, a kinase-like and a tyrosine kinase domain. Genetic and biochemical evidence supports the requirement for tyk2 in interferon-?/? binding and signaling. To study the role of the distinct domains of tyk2, constructs lacking one or both kinase domains were stably transfected in recipient cells lacking the endogenous protein. Removal of either or both kinase domains resulted in loss of the in vitro kinase activity. The mutant form truncated of the tyrosine kinase domain was found to reconstitute binding of interferon-?8 and partial signaling. While no contribution of this protein toward interferon-? binding was evident, increased signaling could be measured. The mutant form lacking both kinase domains did not exhibit any detectable activity. Altogether, these results show that a sequential deletion of domains engenders a sequential loss of function and that the different domains of tyk2 have distinct functions, all essential for full interferon-? and -? binding and signaling. (literal)
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