Granja, A. G., N. D. Perkins, and Y. Revilla. 2008. A238L inhibits NF-ATc2, NF-κB, and c-Jun activation through a novel mechanism involving protein kinase C-θ-mediated up-regulation of the amino-terminal transactivation domain of p300. J. Immunol. 180: 2429-2442.

In Fig. 2B (third panel from the top) the authors inadvertently included the same Western blot panel that is presented in Fig. 2E (third panel from the top). The correct panel for Fig. 2B, representing an immunoprecipitation with anti-p65 followed by a Western blot with anti-p300 Abs, is shown in the figure below.

Replacement for Fig. 2B.

Nuclear extracts from 107 Jurkat-pcDNA and Jurkat-A238L cells treated (+) or not (−) with 15 ng/ml PMA plus 1 μM Ion (PMA/Ion) for 4 h were incubated and immunoprecipitated with 4 μg of rabbit polyclonal specific Ab against NF-κB-p65, as described under Materials and Methods. Immunoprecipitates were separated by SDS-PAGE, electrophoretically transferred to an immobilon membrane, and detected by immunoblotting with p300 (αp300)-specific Ab to detect the interaction between p300 and NF-κB-p65.

Replacement for Fig. 2B.

Nuclear extracts from 107 Jurkat-pcDNA and Jurkat-A238L cells treated (+) or not (−) with 15 ng/ml PMA plus 1 μM Ion (PMA/Ion) for 4 h were incubated and immunoprecipitated with 4 μg of rabbit polyclonal specific Ab against NF-κB-p65, as described under Materials and Methods. Immunoprecipitates were separated by SDS-PAGE, electrophoretically transferred to an immobilon membrane, and detected by immunoblotting with p300 (αp300)-specific Ab to detect the interaction between p300 and NF-κB-p65.

Close modal

In Fig. 8E (second panel from the top), the authors inadvertently scanned and included a horizontally flipped image of the same Western blot that is presented in Fig. 8C (second panel from the top). The correct panel for Fig. 8E, representing an immunoprecipitation with anti–PKC-θ followed by a Western blot with anti–PKC-θ Abs as a PKC immunoprecipitation control, is shown in the figure below.

Replacement for Fig. 8E.

Jurkat-pcDNA and Jurkat-A238L cells were transiently transfected with GAL4-p300 (192–703) wt, as described in Materials and Methods. Twenty-four hours later, the cells were cultured in the absence (−) or presence (+) of PMA/Ion for 2h, and whole-cell extracts were prepared and immunoprecipitated with 4 μg of rabbit polyclonal specific Ab against PKC-θ. Immunoprecipitates were analyzed by Western blot with the same Ab (αPKC-θ) to determine levels of the kinase in the precipitate.

Replacement for Fig. 8E.

Jurkat-pcDNA and Jurkat-A238L cells were transiently transfected with GAL4-p300 (192–703) wt, as described in Materials and Methods. Twenty-four hours later, the cells were cultured in the absence (−) or presence (+) of PMA/Ion for 2h, and whole-cell extracts were prepared and immunoprecipitated with 4 μg of rabbit polyclonal specific Ab against PKC-θ. Immunoprecipitates were analyzed by Western blot with the same Ab (αPKC-θ) to determine levels of the kinase in the precipitate.

Close modal

Data for the densitometry analysis have also been revisited, and no mistakes have been detected. Although incorrect panels were inadvertently included in Figs. 2B and 8E, all the densitometry analysis was performed using the original correct experiments.

The interpretation of data is unaltered and the results and conclusions remain unaffected.