Gu, M., C. Ouyang, W. Lin, T. Zhang, X. Cao, Z. Xia, and X. Wang. 2014. Phosphatase holoenzyme PP1/GADD34 negatively regulates TLR response by inhibiting TAK1 serine 412 phosphorylation. J. Immunol. 192: 2846–2856.

In the original Fig.7B, a blot of p-JNK was used to represent p-ERK1/2 by mistake. In the original Fig.7D, the two right panels for ERK1/2 were inadvertently duplicated.

Fig. 7 appears below with corrected panels (B) and (D). This change does not affect the conclusions or interpretations of findings presented in our article in any way.

FIGURE 7.

TAK1 Ser412 phosphorylation is essential for TLR signaling and production of proinflammatory cytokines. (A) Mouse peritoneal macrophages, RAW264.7, MEF, and C6 cells, were treated by LPS (100 ng/ml for peritoneal macrophages and RAW264.7, 1 μg/ml for MEFs) or IL-1β (10 ng/ml for C6) for the indicated time. Phosphorylation of TAK1 Thr187, Ser412, and total TAK1 were detected by immunoblotting. (B) RAW264.7 cells stably transfected with empty vector (mock), Flag-TAK1, TAK1 T187A, S412A, or K63W were treated with LPS (100 ng/ml) for the indicated time. Cell lysates were immunoblotted with the indicated Abs. (C) RAW264.7 cells were treated with LPS (100 ng/ml), poly-IC (20 μg/ml), or CpG ODN (0.3 μM). IL-6 and TNF-α in the supernatants were measured with ELISA. (D) TAK1−/− MEF cells were transfected with empty vector, TAK1 WT, or the indicated mutants and were treated with LPS (1 μg/ml) for the indicated time. Cell lysates were immunoblotted with indicated Abs. (E) Cells were treated as in (D), but with longer LPS stimulation. Secretion of TNF-α in the supernatant was analyzed by ELISA. Data from (C) and (E) are plotted as means ± SE. All experiments were performed at least three times. *p < 0.05, **p < 0.01, ***p < 0.001 versus controls. ns, no significance.

FIGURE 7.

TAK1 Ser412 phosphorylation is essential for TLR signaling and production of proinflammatory cytokines. (A) Mouse peritoneal macrophages, RAW264.7, MEF, and C6 cells, were treated by LPS (100 ng/ml for peritoneal macrophages and RAW264.7, 1 μg/ml for MEFs) or IL-1β (10 ng/ml for C6) for the indicated time. Phosphorylation of TAK1 Thr187, Ser412, and total TAK1 were detected by immunoblotting. (B) RAW264.7 cells stably transfected with empty vector (mock), Flag-TAK1, TAK1 T187A, S412A, or K63W were treated with LPS (100 ng/ml) for the indicated time. Cell lysates were immunoblotted with the indicated Abs. (C) RAW264.7 cells were treated with LPS (100 ng/ml), poly-IC (20 μg/ml), or CpG ODN (0.3 μM). IL-6 and TNF-α in the supernatants were measured with ELISA. (D) TAK1−/− MEF cells were transfected with empty vector, TAK1 WT, or the indicated mutants and were treated with LPS (1 μg/ml) for the indicated time. Cell lysates were immunoblotted with indicated Abs. (E) Cells were treated as in (D), but with longer LPS stimulation. Secretion of TNF-α in the supernatant was analyzed by ELISA. Data from (C) and (E) are plotted as means ± SE. All experiments were performed at least three times. *p < 0.05, **p < 0.01, ***p < 0.001 versus controls. ns, no significance.

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The figure legend was correct as published and is shown below for reference.