Giovanna Barbieri

TL;DR: Unlike other cytokine receptors studied to date, the receptors for the CNTF cytokine family utilize all known members of the Jak-Tyk family, but induce distinct patterns of Jak- Tyk phosphorylation in different cell lines.

TL;DR: Protein kinases of the Jak family were rapidly tyrosine phosphorylated, and both APRF and Jak1 associated with gp130, indicating that Jak family protein kinases may participate in IL-6 signaling and that APRF may be activated in a complex withgp130.

TL;DR: A cell line is produced which lacks the protein tyrosine kinase JAK1 and is completely defective in interferon response, but implementation of this mutant with JAK2 restored the response, establishing the requirement for JAK 1 in both the interferons-& alpha;/&# 38; beta; and -& #38; gamma; signal transduction pathways.

TL;DR: 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-α and -β binding and signaling.

TL;DR: It is concluded that activation of tyk2 by IFN-alpha does not require an intermediate regulatory tyrosine phosphatase and the effect of pervanadate on the phosphorylation level and the activity of tyK2 is concluded.