Corrections:

Bo Ram Kim¹, Yoon A. Jeong¹, Yoo Jin Na², Seong Hye Park², Min Jee Jo², Jung Lim Kim¹, Soyeon Jeong¹, Suk-Young Lee¹, Hong Jun Kim¹, Sang Cheul Oh^1,2 and Dae-Hee Lee^1,2

¹ Department of Oncology, Korea University Guro Hospital, Seoul, Republic of Korea
² Graduate School of Medicine, Korea University College of Medicine, Seoul, Republic of Korea

Published: June 19, 2018

This article has been corrected: The correct figure 4C is given below:
The authors apologize for the oversight. The authors declare that this correction does not affect the description, interpretation, or the original conclusions of the manuscript.

Original article: Oncotarget. 2017; 8:101952-101964. DOI: https://doi.org/10.18632/oncotarget.21882.

Figure 4: (A) Illustration of the three predicted p53 binding sites in the SMO promoter. The predicted p53 binding sites are presented in the DNA sequence of the SMO promoter (-15000 to -2800). (B) HCT116 cells were treated with 200 μM genipin, and then a chromatin immunoprecipitation (ChIP) assay was performed to con rm the direct binding of p53 to the SMO promoter region. (C) HCT116 cells were treated with 1 μM MG132 for 6 h and 100 μM Leupeptin for 24 h. GLI1 protein expression of was evaluated by western blotting. (D) HCT116 cell lysates were immunoprecipitated with an anti-GLI1 antibody and then immunoblotted with an anti-ubiquitin antibody. (E) The interaction between GLI1 and three E3 ligases was measured by co-immunoprecipitation. HCT116 cell lysates were immunoprecipitated with anti-PCAF, anti-β-TrCP, and anti-ITCH antibodies, and then immunoblotted with an anti-GLI-1 antibody. (F) HCT116 or p53 knockout (KO) HCT116 cells were treated with 200 μM genipin. Lysates of HCT116 and p53 KO HCT116 cells were immunoprecipitated with an anti-GLI1 antibody and immunoblotted with an anti-ubiquitin antibody. Data are expressed as the means of three independent experiments.