Skip to main content
The Journal of Cell Biology logoLink to The Journal of Cell Biology
. 2013 Apr 1;201(1):165. doi: 10.1083/jcb.2011110632011c

Bnip3 and AIF cooperate to induce apoptosis and cavitation during epithelial morphogenesis

Yanmei Qi, Xiaoxiang Tian, Jie Liu, Yaling Han, Alan M Graham, M Celeste Simon, Josef M Penninger, Peter Carmeliet, Shaohua Li
PMCID: PMC3613683

Vol. 198 No. 1, July 9, 2012. Pages 103–114.

The actin panel in the original version of Fig. 5 B was flipped horizontally, and the Fig. 5 B and Fig. 6 C legends did not indicate the intentional duplication of the 3 and 4 d actin data. In addition, the HIF-2α panel in the original version of Fig. 7 C was a duplicate of the HIF-2α panel in Fig. 6 F. The authors have indicated that these issues were due to clerical errors during figure and manuscript preparation. Corrected versions of Fig. 5 B and Fig. 7 C and of the Fig. 5 B and Fig. 6 C legends are shown below.

Figure 5.

Figure 5.

(B) EBs were cultured for 1–4 d and analyzed by immunoblotting for cleaved caspase-3 (cas-3) and actin. Ablation of AIF inhibited caspase-3 activation. The 3 and 4 d actin data are the same as those in Fig. 6 C, where the same blots were analyzed for Bnip3 levels.

Figure 6.

(C) AIFy/+ and AIFy/− EBs were cultured for 3–5 d and analyzed for Bnip3 by immunoblotting. Bnip3 expression was significantly reduced in the absence of AIF. The 3 and 4 d actin data are the same as those in Fig. 5 B, where the same blots were analyzed for cleaved cas-3 levels.

Figure 7.

Figure 7.

(C) 2-d AIFy/+ EBs were treated with or without 2 µM EUK134 for 24 h. Immunoblots show that EUK134 treatment reduced the expression of HIF-1α, HIF-2α, Bnip3, and cleaved caspase-3.

The html and pdf versions of this article have been corrected. The errors remain only in the print version.


Articles from The Journal of Cell Biology are provided here courtesy of The Rockefeller University Press

RESOURCES