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Papers In Press, published online ahead of print November 28, 2002
Immunology Dept., American Red Cross, Rockville, MD 20855
Corresponding Author: keegana{at}usa.redcross.org
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 of time. After IL-4 removal and inhibition of the Jak 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 huIL-4R
J. Biol. Chem, 10.1074/jbc.M211747200
Submitted on November 18, 2002
Revised on November 28, 2002
Accepted on November 28, 2002
Regulation of the dephosphorylation of Stat6: Participation of Y713 in the IL-4R
, the tyrosine phosphatase SHP-1, and the proteasome
in the immunoreceptor tyrosine-based inhibitory motif (ITIM) sequence (Y5F) was dramatically decreased compared to 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 five-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.
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