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Originally published In Press as doi:10.1074/jbc.M211747200 on November 28, 2002

J. Biol. Chem., Vol. 278, Issue 6, 3903-3911, February 7, 2003
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Regulation of the Dephosphorylation of Stat6
PARTICIPATION OF TYR-713 IN THE INTERLEUKIN-4 RECEPTOR alpha , THE TYROSINE PHOSPHATASE SHP-1, AND THE PROTEASOME*

Erica M. HansonDagger §**, Harold Dickensheets, Cheng-Kui Qu||, Raymond P. Donnelly, and Achsah D. KeeganDagger **Dagger Dagger

From the ** Department of Immunology and || Department of Hematopoiesis, Holland Laboratory, American Red Cross, Rockville, Maryland 20855, Dagger  Institute of Biomedical Sciences, George Washington University Medical Center, and  Center for Biologics Evaluation and Research, Federal Drug Administration, Bethesda, Maryland 20892

Signal transducer and activator of transcription 6 (Stat6) plays an important role in interleukin (IL)-4-induced responses. To analyze the regulation of Stat6 phosphorylation, cells were cultured in the continuous presence of IL-4 or after a pulse and washout. In the continual presence of IL-4, Stat6 remained phosphorylated for an extended period. After IL-4 removal and inhibition of the Janus family kinase, tyrosine-phosphorylated Stat6 decayed at a rate dependent upon the length of IL-4 stimulation. The decay of tyrosine-phosphorylated Stat6 was similar in the presence or absence of either cycloheximide or actinomycin D. In the absence of functional Src homology-containing phosphatase-1 (SHP-1), the early loss of tyrosine-phosphorylated Stat6 was substantially reduced. Furthermore, the rate of loss of tyrosine-phosphorylated Stat6 in cells expressing a mutation of the human IL-4 receptor alpha  in the immunoreceptor tyrosine-based inhibitory motif sequence (Y5F) was dramatically decreased compared with wild-type cells. The early rate of decay was similar in the presence or absence of MG132, an inhibitor of the proteasome, but the later rate of decay was decreased 5-fold. These results suggest that the loss of tyrosine phosphorylation of Stat6 is regulated by the action of SHP-1 and the proteasome but is not dependent on new protein synthesis.

* This work was supported by National Institutes of Health Grant AI38985 (to A. D. K.), by The George Washington Institute of Biomedical Sciences (to E. M. H.), and by the American Red Cross.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.

§ Submitted this work in partial fulfillment of the requirements for the Doctor of Philosophy degree, Immunology Program, Institute for Biomedical Sciences of the Columbian School of Arts and Sciences, The George Washington University.

Dagger Dagger To whom correspondence should be addressed: Dept. of Immunology, Holland Laboratory, American Red Cross, 15601 Crabbs Branch Way, Rockville, MD 20855. Tel.: 301-517-0326; Fax: 301-517-0344; E-mail: KeeganA@usa.redcross.org.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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