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. 2016 Dec 1;17(12):1901. doi: 10.15252/embr.201570010

Sulfatase activities are regulated by the interaction of the sulfatase‐modifying factor 1 with SUMF2

Ester Zito, Alessandro Fraldi, Stefano Pepe, Ida Annunziata, Gary Kobinger, Paola Di Natale, Andrea Ballabio, Maria Pia Cosma
PMCID: PMC5283596  PMID: 27909074

Abstract

graphic file with name EMBR-17-1901-g001.jpg

Authors’ statement

Following a note from the authors to EMBO Reports and subsequent investigation by the Journal, the following errors are reported:

We have come to realize that bands in Supplementary Fig 4A and B were derived from different gels and pasted on white background. Furthermore, several bands in Supplementary Fig 4A and B appear to be possible duplications (in particular, the bands in lanes 2, 6, 7 top panel of A and lane 2, bottom panel of B may have been duplicated; lane 7 bottom panel of A and lane 4, bottom panel of B may have been duplicated; lanes 5 and 6, bottom panel of A may have been duplicated), although this cannot be concluded unequivocally due to the low resolution of the figure. Supplementary Fig 4A and B displays loading controls of the co‐IP experiments shown in Fig 2A and C. These results, however, are not essential to support the main conclusion of Fig 2A and C, namely that SUMF1 and SUMF2 interact with themselves and with IDS and SGSH, because the reported interactions involved expression of tagged factors and, therefore, the interactions are unequivocally documented by anti‐tag‐specific antibodies. Furthermore, these interactions are confirmed by other results in the publication (mainly by the co‐IP experiment using differently tagged proteins in Supplementary Fig 3A, by the co‐IP of the endogenous proteins in Fig 2B, as well as by the experiments showing cysteine‐mediated interactions in Fig 3), through an unbiased mass spec method 1 and by others 2.

As source data are unfortunately no longer available and the content of these Supplementary Figures is not necessary for the conclusions of Fig 2A and B, we would like that Supplementary Fig 4A and B is considered withdrawn from the paper.

All authors concur with this statement and wish to apologize for the inconvenience caused.

Editors’ statement

In light of the potential image aberrations noted in the author’s statement, and since source data were not available for this figure, panels A and B of Supplementary Fig 4 are herewith retracted. These panels constituted loading controls for Fig 2A and C with limited impact on the qualitative conclusions made in the paper—see author statement for further details.

We alert readers to the fact that one related paper at The EMBO Journal is also subject to a correction:

Zito E, Buono M, Pepe S, Settembre C, Annunziata I, Surace EM, Dierks T, Monti M, Cozzolino M, Pucci P, Ballabio A, Cosma MP (2007) Sulfatase modifying factor 1 trafficking through the cells: from endoplasmic reticulum to the endoplasmic reticulum. EMBO J 26: 2443–2453

References

  • 1. Fraldi A, Zito E, Annunziata F, Lombardi A, Cozzolino M, Monti M, Spampanato C, Ballabio A, Pucci P, Sitia R et al (2008) Multistep, sequential control of the trafficking and function of the multiple sulfatase deficiency gene product, SUMF1 by PDI, ERGIC‐53 and ERp44. Hum Mol Genet 17: 2610–2621 [DOI] [PubMed] [Google Scholar]
  • 2. Dickmanns A, Schmidt B, Rudolph MG, Mariappan M, Dierks T, von Figura K, Ficner R (2005) Crystal structure of human pFGE, the paralog of the Calpha‐formylglycine‐generating enzyme. J Biol Chem 280: 15180–15187 [DOI] [PubMed] [Google Scholar]

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