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The Journal of Immunology, Vol 159, Issue 3 1255-1264, Copyright © 1997 by American Association of Immunologists
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B Lu, M Reichel, DA Fisher, JF Smith and P Rothman
Integrated Program in Molecular, Cellular, and Biophysical Studies, College of Physicians and Surgeons, Columbia University, New York, NY 10032, USA.
Tyrosine phosphorylation of STAT6 in response to IL-4 results in the formation of STAT6 homodimers that bind specific DNA elements. Although binding sites for STAT6 have been shown to be important for the function of several IL-4-inducible promoters, the role of STAT6 in this activation has not been defined. To determine whether STAT6 is a transcriptional activator, different portions of the carboxyl terminus of STAT6 were fused to the yeast Gal4 protein DNA binding domain. Analysis of these chimeric Gal4-STAT6 proteins demonstrates that a 140- amino-acid proline-rich region of the carboxyl terminus of STAT6 contains a region that activates transcription. Truncation mutants of STAT6 that lack this domain cannot activate transcription and are capable of repressing transcription stimulated by a wild-type STAT6 protein. Strikingly, the ability of IL-4 to induce transcription from the Ig germline epsilon promoter is suppressed by overexpression of a carboxyl-terminal deletion mutant of STAT6. These studies demonstrate that the carboxyl terminus of STAT6 contains an activating domain required for the induction of genes by IL-4.
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J. S. Nair, C. J. DaFonseca, A. Tjernberg, W. Sun, J. E. Darnell Jr., B. T. Chait, and J. J. Zhang Requirement of Ca2+ and CaMKII for Stat1 Ser-727 phosphorylation in response to IFN-gamma PNAS, April 30, 2002; 99(9): 5971 - 5976. [Abstract] [Full Text] [PDF]
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C. J. DaFonseca, F. Shu, and J. J. Zhang Identification of two residues in MCM5 critical for the assembly of MCM complexes and Stat1-mediated transcription activation in response to IFN-gamma PNAS, March 13, 2001; 98(6): 3034 - 3039. [Abstract] [Full Text] [PDF]
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