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Originally published In Press as doi:10.1074/jbc.M101219200 on April 6, 2001

J. Biol. Chem., Vol. 276, Issue 25, 23173-23178, June 22, 2001
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Specific Dephosphorylation of the Lck Tyrosine Protein Kinase at Tyr-394 by the SHP-1 Protein-tyrosine Phosphatase*

Gary G. ChiangDagger § and Bartholomew M. SeftonDagger

From the Dagger  Molecular and Cell Biology Laboratory, The Salk Institute for Biological Studies, La Jolla, California, 92037 and the § Division of Biology, University of California, San Diego, La Jolla, California 92093

The protein-tyrosine phosphatase SHP-1 has been shown to be a negative regulator of multiple signaling pathways in hematopoietic cells. In this study, we demonstrate that SHP-1 dephosphorylates the lymphoid-specific Src family kinase Lck at Tyr-394 when both are transiently co-expressed in nonlymphoid cells. We also demonstrate that a GST-SHP-1 fusion protein specifically dephosphorylates Lck at Tyr-394 in vitro. Because phosphorylation of Tyr-394 activates Lck, the fact that SHP-1 specifically dephosphorylates this site suggests that SHP-1 is a negative regulator of Lck. The failure of SHP-1 to inactivate Lck may contribute to some of the lymphoid abnormalities observed in motheaten mice.

* This work was supported in part by Grants CA14195 and CA42350 from NCI, the National Institutes of Health.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 Training Grant T32-CA09435 from NCI, the National Institutes of Health and fellowships from the Chapman Charitable Trust and the Salk Institute Association. To whom correspondence should be addressed: Molecular and Cell Biology Laboratory, The Salk Inst., 10010 N. Torrey Pines Rd., La Jolla, CA 92037. Tel.: 858-453-4100, Ext. 1331; Fax: 858-457-4765; E-mail: chiang@salk.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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