TY - JOUR
T1 - Corrigendum to
T2 - Sulphatase activities are regulated by the interaction of sulphatase-modifying factor 1 with SUMF2 (EMBO reports, (2005), 6, 7, (655-660), 10.1038/sj.embor.7400454)
AU - Zito, Ester
AU - Fraldi, Alessandro
AU - Pepe, Stefano
AU - Annunziata, Ida
AU - Kobinger, Gary
AU - Di Natale, Paola
AU - Ballabio, Andrea
AU - Cosma, Maria Pia
N1 - Publisher Copyright:
© 2016 The Authors.
PY - 2016/12/1
Y1 - 2016/12/1
N2 - 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 antitag- 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is not necessary for the conclusions of Fig 2A and B, we would like that Supplementary Fig 4A and B is considered withdrawn from the paper.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.
AB - 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 antitag- 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.
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U2 - 10.15252/embr.201570010
DO - 10.15252/embr.201570010
M3 - Comment/debate
AN - SCOPUS:84999854458
SN - 1469-221X
VL - 17
SP - 1901
JO - EMBO reports
JF - EMBO reports
IS - 12
ER -