First Author | Lu B | Year | 1997 |
Journal | J Immunol | Volume | 159 |
Issue | 3 | Pages | 1255-64 |
PubMed ID | 9233621 | Mgi Jnum | J:41638 |
Mgi Id | MGI:894168 | Doi | 10.4049/jimmunol.159.3.1255 |
Citation | Lu B, et al. (1997) Identification of a STAT6 domain required for IL-4-induced activation of transcription. J Immunol 159(3):1255-64 |
abstractText | 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. |