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Originally published In Press as doi:10.1074/jbc.M109165200 on December 18, 2001

J. Biol. Chem., Vol. 277, Issue 10, 8673-8681, March 8, 2002
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SH2-B Family Members Differentially Regulate JAK Family Tyrosine Kinases*

Karen B. O'BrienDagger §, John J. O'Shea, and Christin Carter-SuDagger ||

From the Dagger  Department of Physiology, University of Michigan Medical School, Ann Arbor, Michigan 48109-0622 and  NIAMS, National Institutes of Health, Bethesda, Maryland 28092-1820

Activation of JAK tyrosine kinases is an essential step in cell signaling by multiple hormones, cytokines, and growth factors, including growth hormone (GH) and interferon-gamma . Previously, we identified SH2-Bbeta as a potent activator of JAK2 (Rui, L., and Carter-Su, C. (1999) Proc. Natl. Acad. Sci. U. S. A. 96, 7172-7177). Here, we investigated whether the activation of JAK2 by SH2-Bbeta is specific to JAK2 and SH2-Bbeta or extends to other JAKs or other members of the SH2-Bbeta family. When SH2-Bbeta was overexpressed with JAK1 or JAK3, SH2-Bbeta failed to increase their activity. However, SH2-Bbeta bound to both and was tyrosyl-phosphorylated by JAK1. In contrast to SH2-Bbeta , APS decreased tyrosyl phosphorylation of GH-stimulated JAK2 as well as Stat5B, a substrate of JAK2. APS also decreased tyrosyl phosphorylation of JAK1, but did not affect the activity or tyrosyl phosphorylation of JAK3. Overexpressed APS bound to and was tyrosyl-phosphorylated by all three JAKs. Consistent with these data, in 3T3-F442A adipocytes, endogenous APS was tyrosyl-phosphorylated in response to GH and interferon-gamma . These results suggest that 1) SH2-Bbeta specifically activates JAK2, 2) APS negatively regulates both JAK2 and JAK1, and 3) both SH2-Bbeta and APS may serve as adapter proteins for all three JAKs independent of any role they have in JAK activity.

* This work was supported in part by National Institutes of Health Grants DK34171 and DK54222.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ Supported by a predoctoral fellowship from the University of Michigan Cancer Center (National Institutes of Health Training Grant 5T32CAO96760). Student in the Cellular and Molecular Biology Graduate Program at the University of Michigan.

|| To whom correspondence should be addressed: Dept. of Physiology, University of Michigan Medical School, 6804 Medical Science II, 1301 E. Catherine St., Ann Arbor, MI 48109-0622. Tel.: 734-763-2561; Fax: 734-647-9523; E-mail: cartersu@umich.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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