Corrigendum: Contrasting effects on HIF-1α regulation by disease-causing pVHL mutations correlate with patterns of tumourigenesis in von Hippel-Lindau disease

In the originally published version of this article there was an error in Figure 2B with inadvertent duplication of the images for the Ser80Gln and Leu188Val pVHL mutants. A corrected figure that matches the format of the original paper had been prepared from the autoradiographs of experiments performed at the same time as the original experiments (the original autoradiographs could not be located). The corrected Figure 2 shown here demonstrates that only wild-type pVHL (1-213 and 54-213) and type 2C mutants were able to re-constitute pVHL-dependent HIF-1α ubiquitylation activity, as was the case in the original. This is evident from the appearance of a low mobility HIF-1α ubiquitylated species (HIF-1α/ubq) coupled with a marked reduction in the non-ubiquitylated HIF-1α species. The findings and conclusions of the experiments are unchanged and have only been corrected in this corrigendum to preserve the published version of record. Nevertheless, the authors apologize for the error.

Figure 2

Re-constitution of HIF-1α ubiquitylation activity in vitro by pVHL mutants. The ability of exogenously added in vitro transcribed-translated pVHL products to re-constitute pVHL-dependent HIF-1α ubiquitylation activity in VHL (-/-) RCC4 cell extracts is shown. Panels show results from a single experiment on two SDS-PAGE gels (A and B) with irrelevant lanes removed. All pVHL constructs shown are C-terminally HA epitope-tagged (Materials and Methods). Disease phenotypes associated with each mutation are also shown (1, 2A, 2B, 2C). Only wild-type pVHL (1-213 and 54-213) and type 2C mutants were able to re-constitute pVHL-dependent HIF-1α ubiquitylation activity, as observed by the appearance of a low mobility HIF-1α ubiquitylated species (HIF-1α/ubq) coupled with a marked reduction in the non-ubiquitylated HIF-1α species. Input pVHL species are observed on the lower portion of the gels, showing equivalent loading between pVHL constructs [note that all pVHL products contain three methionine residues except for WT (54-213) and GLN 195 TER, which contain two]. In panel A, all samples are shown following 90 min incubation at 30^ΰC, except lane 1 (left side) on each gel, which represents time-point zero (T0); in panel B incubation times (min) are as indicated.