The amino-terminal region of Tyk2 sustains the level of interferon a receptor 1, a component of the interferon a/b receptor. (Articolo in rivista)

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  • The amino-terminal region of Tyk2 sustains the level of interferon a receptor 1, a component of the interferon a/b receptor. (Articolo in rivista) (literal)
Anno
  • 1997-01-01T00:00:00+01:00 (literal)
Alternative label
  • Gauzzi MC *, Barbieri G *, Richter MF *, Uzé G §, Ling L ¶, Fellous M * and Pellegrini S * (1997)
    The amino-terminal region of Tyk2 sustains the level of interferon a receptor 1, a component of the interferon a/b receptor.
    in Proceedings of the National Academy of Sciences of the United States of America; Hidesaburo Hanafusa, The Rockefeller University, New York, NY (Stati Uniti d'America)
    (literal)
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  • Gauzzi MC *, Barbieri G *, Richter MF *, Uzé G §, Ling L ¶, Fellous M * and Pellegrini S * (literal)
Pagina inizio
  • 11839 (literal)
Pagina fine
  • 11844 (literal)
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  • 94 (literal)
Rivista
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  • 5 (literal)
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  • Google Scholar (literal)
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  • *Institut Pasteur, Institut National de la Santé et de la Recherche Medicale Unité 276, Paris 75724 Cedex 15, France; §Institut de Genetique Moleculaire, Centre National de la Recherche Scientifique, Unite Mixe de Recherche 9942, Montpellier, France; and ¶Biogen, Inc., Cambridge, MA 02142 (literal)
Titolo
  • The amino-terminal region of Tyk2 sustains the level of interferon a receptor 1, a component of the interferon a/b receptor. (literal)
Abstract
  • Tyk2 belongs to the Janus kinase (JAK) family of receptor associated tyrosine kinases, characterized by a large N-terminal region, a kinase-like domain and a tyrosine kinase domain. It was previously shown that Tyk2 contributes to interferon-a (IFN-a) signaling not only catalytically, but also as an essential intracellular component of the receptor complex, being required for high affinity binding of IFN-a. For this function the tyrosine kinase domain was found to be dispensable. Here, it is shown that mutant cells lacking Tyk2 have significantly reduced IFN-a receptor 1 (IFNAR1) protein level, whereas the mRNA level is unaltered. Expression of the N-terminal region of Tyk2 in these cells reconstituted wild-type IFNAR1 level, but did not restore the binding activity of the receptor. Studies of mutant Tyk2 forms deleted at the N terminus indicated that the integrity of the N-terminal region is required to sustain IFNAR1. These studies also showed that the N-terminal region does not directly modulate the basal autophosphorylation activity of Tyk2, but it is required for efficient in vitro IFNAR1 phosphorylation and for rendering the enzyme activatable by IFN-a. Overall, these results indicate that distinct Tyk2 domains provide different functions to the receptor complex: the N-terminal region sustains IFNAR1 level, whereas the kinase-like domain provides a function toward high affinity ligand binding. (literal)
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