Nucleic Acids Research, Vol 27, Issue 13 2722-2729, Copyright © 1999 by Oxford University Press
S Gingras, J Simard, B Groner and E Pfitzner
Interleukin-4 (IL-4) induces tyrosine phosphorylation of the latent
transcription factor Stat6, which mediates the transcriptional responses of
IL-4. The transactivation domain of Stat6 has recently been mapped to the
C-terminal region of Stat6. We have investigated the mechanism by which
Stat6, through its transactivation domain, induces transcription. Previous
studies have shown that diverse regulated transcription factors interact
with coactivators such as p300 and CBP. We report that Stat6 used the
interaction with p300/CBP to exert its stimulatory effects. Overexpression
of p300/CBP increased IL-4-induced transcription of Stat6 activated
reporter genes. The requirement of p300/CBP for Stat6-mediated
transactivation is shown by coexpression of the adenovirus E1A protein. E1A
repressed the IL-4-induced reporter gene activity, while mutants of E1A,
which do not interact with p300/CBP, failed to block the IL-4-induced
response. In addition, we found that the minimal transactivation domain of
Stat6, when fused to the GAL4 DNA-binding domain, was repressed by E1A,
whereas the fusion protein p300-VP16 increased the transcriptional
activity. In two-hybrid protein interaction assays in mammalian cells, we
mapped the interaction domain of CBP to a C-terminal region between amino
acids 1850 and 2176, a region distinct from the interaction domain of CBP
with Stat1, Stat2 or Stat5. Finally, we show that antibodies raised against
p300 coimmunoprecipitated Stat6 and p300 from transfected COS7 cells and
antibodies against Stat6 coimmunprecipitated endogenous Stat6 and CBP from
Ba/F3 cells. Our data suggest that the transactivation domain of Stat6
makes contact with the basal transcription machinery by binding to
p300/CBP.
ARTICLES
p300/CBP is required for transcriptional induction by interleukin-4 and interacts with Stat6
Medical Research Council Group in Molecular Endocrinology, CHUL Research Center and Laval University, 2705 Laurier Boulevard, Quebec City G1V 4G2, Canada.
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