The authors of the original article “Proteasome and thiol involvement in quality control of glycosylphosphatidylinositol anchor addition” DOI: 10.1042/bj3320111: Wilbourn et al., Biochem. J.332, 111–118 (1998) would like to correct Figure 5 of this article. After publication, a reader identified that Figure 5 contained a duplicated Western blot image in panel ‘B’ between the “28” and “29” experimental groups. The authors confirmed that the “28” Western blot image was inadvertently duplicated and re-used for the "29" control experiment. The authors state that due to the age of this article, the original image data can no longer be accessed, and have therefore elected to correct Figure 5 by removing the duplicated Western blot image in Figure 5B and the associated analysis of hGHDAF29 in Figure 5A.

In addition, the following text in the section: “Effect of mutations on hGHDAF28 kinetics” in the Results has been corrected from: “In stark contrast to hGHDAF28, hGHDAF28 R4, hGHDAF28 KDEL and hGHDAF29, ∼60 % hGHDAF28 C203S was recovered efficiently from the medium after 3 h (Figure 5). A small amount of hGHDAF29 was also found in the medium, but is probably due to shedding of this GPI-anchored protein from the cell surface.” to: “In stark contrast to hGHDAF28, hGHDAF28 R4 and hGHDAF28 KDEL, ∼60 % hGHDAF28 C203S was recovered efficiently from the medium after 3 h (Figure 5).” to reflect the updated Figure 5.

Figure 1.
Mutation of Cys-203 in the C-terminus of hGHDAF28 leads to secretion.

CHO cells expressing hGHDAF fusion proteins were pulse-labelled for 1 h. The medium was removed and replaced with complete medium and the cells were incubated for a further 3 h. After that time the cells and the media were harvested and analysed. (A) Quantification of immunoprecipitation data showing that hGHDAF28[C203S is secreted. Data are the means of two experiments. (B) Representative gel images used for quantification. Lanes: M, medium; C, cell lysate.

Figure 1.
Mutation of Cys-203 in the C-terminus of hGHDAF28 leads to secretion.

CHO cells expressing hGHDAF fusion proteins were pulse-labelled for 1 h. The medium was removed and replaced with complete medium and the cells were incubated for a further 3 h. After that time the cells and the media were harvested and analysed. (A) Quantification of immunoprecipitation data showing that hGHDAF28[C203S is secreted. Data are the means of two experiments. (B) Representative gel images used for quantification. Lanes: M, medium; C, cell lysate.

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The requested correction has been assessed and agreed by the Editorial Board. The authors declare that these corrections do not change the conclusions of their paper, and would like to highlight that the affected results with hGHDAF29 were repeat (control) analyses from a previous study by Moran et al 1992 (DOI: 10.1083/jcb.119.4.763). The corrected version of Figure 5 is presented here.