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Proceedings of the National Academy of Sciences of the United States of America logoLink to Proceedings of the National Academy of Sciences of the United States of America
. 1998 Oct 13;95(21):12734.
PMCID: PMC56075

Medical Sciences. In the article “CREB binding protein is a required coactivator for Smad-dependent, transforming growth factor β transcriptional responses in endothelial cells” by James N. Topper, Maria R. DiChiara, Jonathan D. Brown, Amy J. Williams, Dean Falb, Tucker Collins, and Michael A. Gimbrone, Jr., which appeared in number 16, August 4, 1998, of Proc. Natl. Acad. Sci. USA 95, 9506–9511), the following correction should be noted. The graphics, but not the corresponding legends, of Figs. 4 and 6 have been inadvertantly transposed. The corrected figures and corresponding legends are shown below.

Figure 4.

Figure 4

Smads 2 and 4 can interact with CBP in vivo. Cos-7 cells were transfected with the indicated combinations of epitope-tagged activated TBF-β type-1 receptor, Smad expression construct, or empty expression vector. The cells were then lysed and immunoprecipitated with an anti-CBP/P300 antisera. Coprecipitating Smad proteins were detected by Western blot. The upper two panels demonstrate that significant amounts of both Smad2 and Smad4 protein coimmunoprecipitate with CBP/P300 in the presence of the activated receptor. These interactions are inhibited by the simultaneous expression of either Smad6 or Smad7 but not by cotransfection of an empty expression vector (pCIneo). The bottom panels confirm comparable Smad2, Smad4, and activated receptor expression by immunoprecipitation and Western blotting with antisera against the epitopes fused to these proteins.

Figure 6.

Figure 6

12S E1A inhibits the association of activated Smad2 and Smad4 with CBP in vivo. Cos-7 cells were transfected with expression constructs expressing epitope-tagged (HA, Flag) versions of Smad2 and Smad4 and the indicated combinations of activated TBF-β type-1 receptor and 12S E1A expression vector. The cells were subsequently lysed and subjected to immunoprecipitation with anti-CBP/p300 antisera, and levels of coimmunoprecipitating Smad proteins were determined by Western blot. The bottom panels confirm comparable Smad2, Smad4, and activated receptor expression.


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