There was an error in J. Cell Sci. (2010) 123, 4251-4258(doi:10.1242/jcs.073783).

The journal was informed that the p65 and myc (p65) blots in Fig. 1A,B are identical to those shown in fig. 3A,B of another paper by the same authors in BMC Genomics (2010) 11, 22 (doi:10.1186/1471-2164-11-22). The authors explained that the data in the two figures validate the specificity of antibodies generated against different acetylated lysines of p65 and originate from the same experiment, meaning that use of the same controls is justified. Although the BMC Genomics paper was referenced and discussed, the authors should have stated in the legend for Fig. 1 that these control blots were reproduced from their earlier paper. The corrected and original legends are shown below and the online full-text and PDF versions of the paper have been updated.

Fig. 1. (corrected) Kinetics of p65 K310 acetylation upon TNFα stimulation. (A,B) Characterization of specific antibody against p65 acetylated at K310. (A) Purified recombinant p65 wild type and the acetylation-deficient mutants were incubated with recombinant p300 in the presence (+) or absence (−) of acetyl CoA. Proteins were resolved by SDS-PAGE and analyzed by western blot using the indicated antibodies. (B) HEK293T cells were transfected with p65 wild type or mutants, with (+) or without (−) p300 co-transfection. Acetylation of p65 at specific K310 was assessed by western blot using the specific antibody. Note that the control p65 blot in A and the control myc (p65) blot in B are reproduced from fig. 3 in Rothgeisser et al. (2010); the data shown here are part of a larger experiment to validate antibodies specific to acetylated p65. (C,D) Endogenous p65 is rapidly and possibly transiently acetylated in the nucleus upon TNFα stimulation in vivo. (C) Wild-type p65 complemented MEFs were treated with TNFα for the indicated time periods. p65 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-acetyl K310 antibody. PARP1 from 5% input was used as nuclear loading control. (D) Wild-type or K310R p65 complemented MEFs were treated with TNFα for the indicated time periods. Acetyl K310 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-p65 antibody. PARP1 from 2.5% input was used as nuclear loading control.

Fig. 1. (corrected) Kinetics of p65 K310 acetylation upon TNFα stimulation. (A,B) Characterization of specific antibody against p65 acetylated at K310. (A) Purified recombinant p65 wild type and the acetylation-deficient mutants were incubated with recombinant p300 in the presence (+) or absence (−) of acetyl CoA. Proteins were resolved by SDS-PAGE and analyzed by western blot using the indicated antibodies. (B) HEK293T cells were transfected with p65 wild type or mutants, with (+) or without (−) p300 co-transfection. Acetylation of p65 at specific K310 was assessed by western blot using the specific antibody. Note that the control p65 blot in A and the control myc (p65) blot in B are reproduced from fig. 3 in Rothgeisser et al. (2010); the data shown here are part of a larger experiment to validate antibodies specific to acetylated p65. (C,D) Endogenous p65 is rapidly and possibly transiently acetylated in the nucleus upon TNFα stimulation in vivo. (C) Wild-type p65 complemented MEFs were treated with TNFα for the indicated time periods. p65 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-acetyl K310 antibody. PARP1 from 5% input was used as nuclear loading control. (D) Wild-type or K310R p65 complemented MEFs were treated with TNFα for the indicated time periods. Acetyl K310 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-p65 antibody. PARP1 from 2.5% input was used as nuclear loading control.

Fig. 1. (original) Kinetics of p65 K310 acetylation upon TNFα stimulation. (A,B) Characterization of specific antibody against p65 acetylated at K310. (A) Purified recombinant p65 wild type and the acetylation-deficient mutants were incubated with recombinant p300 in the presence (+) or absence (−) of acetyl CoA. Proteins were resolved by SDS-PAGE and analyzed by western blot using the indicated antibodies. (B) HEK293T cells were transfected with p65 wild type or mutants, with (+) or without (−) p300 co-transfection. Acetylation of p65 at specific K310 was assessed by western blot using the specific antibody. (C,D) Endogenous p65 is rapidly and possibly transiently acetylated in the nucleus upon TNFα stimulation in vivo. (C)Wild-type p65 complemented MEFs were treated with TNFα for the indicated time periods. p65 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-acetyl K310 antibody. PARP1 from 5% input was used as nuclear loading control. (D) Wild-type or K310R p65 complemented MEFs were treated with TNFα for the indicated time periods. Acetyl K310 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-p65 antibody. PARP1 from 2.5% input was used as nuclear loading control.

Fig. 1. (original) Kinetics of p65 K310 acetylation upon TNFα stimulation. (A,B) Characterization of specific antibody against p65 acetylated at K310. (A) Purified recombinant p65 wild type and the acetylation-deficient mutants were incubated with recombinant p300 in the presence (+) or absence (−) of acetyl CoA. Proteins were resolved by SDS-PAGE and analyzed by western blot using the indicated antibodies. (B) HEK293T cells were transfected with p65 wild type or mutants, with (+) or without (−) p300 co-transfection. Acetylation of p65 at specific K310 was assessed by western blot using the specific antibody. (C,D) Endogenous p65 is rapidly and possibly transiently acetylated in the nucleus upon TNFα stimulation in vivo. (C)Wild-type p65 complemented MEFs were treated with TNFα for the indicated time periods. p65 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-acetyl K310 antibody. PARP1 from 5% input was used as nuclear loading control. (D) Wild-type or K310R p65 complemented MEFs were treated with TNFα for the indicated time periods. Acetyl K310 was immunoprecipitated from nuclear extracts and analyzed by western blot using anti-p65 antibody. PARP1 from 2.5% input was used as nuclear loading control.

The authors apologise to readers for this omission, which does not impact the results or conclusions of the paper.