Correction to: Oncogene; 10.1038/onc.2013.573; published online 20 January 2014.
Since the publication of the above article, the authors have noted that the input data in Fig. 6E is incorrect. The correct data are included in the below Fig. 6E. The mistake does not affect the conclusions of the paper as the levels of input proteins remain similar between samples. We apologise for any inconvenience caused by this error.
Fig. 6.
RNF31 triggers ERα mono-ubiquitination. a Detection of a potentially mono-ubiquitinated form of ERα upon RNF31 overexpression. HEK-293 cells were transfected with ERα together with plasmids expressing Myc-tagged RNF31 or the Myc-tag alone. Forty-eight hours after transfection, whole-cell extracts were prepared and levels of ERα protein assayed by western blot analysis. The predicted molecular weights of RNF31, ERα, mono-ubiquitinated ERα and of the internal control GAPDH are indicated. b Detection of endogenous mono-ubiquitinated ERα upon RNF31 depletion. MCF-7 cells were transfected with siRNF31 or siControl. Forty-eight hours after transfection, whole-cell extracts were prepared and levels of ERα protein assayed by western blot analysis. The predicted molecular weights of RNF31, ERα, mono-ubiquitinated ERα and the internal control GAPDH are indicated. c Deletion of the RNF31 RBR domain abolishes the potentially mono-ubiquitinated form of ERα. HEK-293 cells were transfected with ERα together with plasmids expressing Myc-tagged full-length RNF31 derivatives or the Myc-tag alone. Forty-eight hours post transfection, cell extracts were prepared and ERα forms were detected by western blot analysis. The predicted molecular weights of RNF31, ERα, mono-ubiquitinated ERα and of the internal control GAPDH are indicated. d Direct evidence for ERα mono-ubiquitination. Immunoprecipitation of ubiquitinated proteins from MCF-7 cell extracts upon overexpression of RNF31. Ubiquitinated ERα species were detected by western blots using anti-ERα, identifying a prominent 75 kDa mono-ubiquitinated ER form. e ERα mono-ubiquitination requires the RNF31 RBR domain. Plasmids expressing Myc-tagged RNF31 derivatives were transfected into HEK-293 cells together with the ERα expression plasmid. Whole-cell extracts were subjected to immunoprecipitation of ERα and subsequently analyzed for ubiquitinated ERα forms by western blot analysis using anti-ubiquitin. The predicted molecular weight of mono-ubiquitinated ERα is indicated