Note to users. If you're seeing this message, it means that your browser cannot find this page's style/presentation instructions -- or possibly that you are using a browser that does not support current Web standards. Find out more about why this message is appearing, and what you can do to make your experience of our site the best it can be.


Sci. STKE, 16 May 2000
Vol. 2000, Issue 32, p. tw11
[DOI: 10.1126/stke.2000.32.tw11]

EDITORS' CHOICE

Nonreceptor Tyrosine Kinases Functions for the Pseudokinase Domain

Jak2 is a nonreceptor tyrosine kinase involved in transducting signals from cytokine receptors. Saharinen et al. demonstrate that the JH2 domain, which is a pseudokinase domain, negatively regulates the activity of Jak2 by transfecting cells with a variety of mutant Jak2 constructs. Deletion of the JH2 domain had several effects: (i) increased tyrosine phosphorylation of Jak, (ii) increased Jak kinase activity, (iii) increased phosphorylation of STAT5 along with loss of dependence on the SH2 domain of STAT5 for phosphorylation, and (iv) activated a STAT reporter gene in a ligand-independent manner. Their data support an intramolecular interaction between the JH1 kinase domain and the JH2 pseudokinase domain that regulates kinase activity and substrate recognition.

Saharinen, P., Takaluoma, K., and Silvennionen, O. (2000) Regulation of the Jak2 tyrosine kinase by its pseudokinase domain. Mol. Cell. Biol. 20: 3387-3395. [Abstract] [Full Text]

Citation: Functions for the Pseudokinase Domain. Sci. STKE 2000, tw11 (2000).


To Advertise     Find Products


Science Signaling. ISSN 1937-9145 (online), 1945-0877 (print). Pre-2008: Science's STKE. ISSN 1525-8882