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Originally published In Press as doi:10.1074/jbc.M207127200 on August 6, 2002

J. Biol. Chem., Vol. 277, Issue 42, 39274-39279, October 18, 2002
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Regulation of the EphA2 Kinase by the Low Molecular Weight Tyrosine Phosphatase Induces Transformation*

Keith D. KikawaDagger , Derika R. Vidale§, Robert L. Van Etten§, and Michael S. KinchDagger ||

From the Departments of Dagger  Basic Medical Sciences and § Chemistry, Purdue University, West Lafayette, Indiana 47907 and  MedImmune, Inc., Gaithersburg, Maryland 20878

Intracellular signaling by protein tyrosine phosphorylation is generally understood to govern many aspects of cellular behavior. The biological consequences of this signaling pathway are important because the levels of protein tyrosine phosphorylation are frequently elevated in cancer cells. In the classic paradigm, tyrosine kinases promote tumor cell growth, survival, and invasiveness, whereas tyrosine phosphatases negatively regulate these same behaviors. Here, we identify one particular tyrosine phosphatase, low molecular weight tyrosine phosphatase (LMW-PTP), which is frequently overexpressed in transformed cells. We also show that overexpression of LMW-PTP is sufficient to confer transformation upon non-transformed epithelial cells. Notably, we show that the EphA2 receptor tyrosine kinase is a prominent substrate for LMW-PTP and that the oncogenic activities of LMW-PTP result from altered EphA2 expression and function. These results suggest a role for LMW-PTP in transformation progression and link its oncogenic potential to EphA2.

* This work was supported by from National Institutes of Health Grants 1 U01 CA91318 (to M. K.) and GM27003 (to R. V. E.) and by grants from the Department of Defense Breast and Prostate Cancer Research Programs.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.

|| To whom correspondence should be addressed: MedImmune, Inc., 35 West Watkins Mill Rd., Gaithersburg, MD 20878. Tel.: 240-632-4639; Fax: 301-527-4200; E-mail: kinchm@medimmune.com.

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