Erratum
for Dimitrov et al., Hum. Mol. Genet. 18 (3) 440-453.
Human Molecular Genetics Advance Access published online on February 16, 2009
Human Molecular Genetics, doi:10.1093/hmg/ddp062
© The Author 2009. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org
The gene responsible for Dyggve-Melchior-Clausen syndrome encodes a novel peripheral membrane protein dynamically associated with the Golgi apparatus
Ariane Dimitrov,
Vincent Paupe,
Charles Gueudry,
Jean-Baptiste Sibarita,
Graça Raposo,
Ole Vielemeyer,
Thierry Gilbert,
Zsolt Csaba,
Tania Attie-Bitach,
Valérie Cormier-Daire,
Pierre Gressens,
Pierre Rustin,
Franck Perez and
Vincent El Ghouzzi
Human Molecular Genetics 2009 18:3; pp. 440–453 doi:10.1093/hmg/ddn371
The Publisher and Authors would like to apologise for errors in Figures 3 and 6, respectively. Figure 3 was enlarged, as a consequence the right hand side of the figure was cropped. In Figure 6, the figure parts were labelled incorrectly. The complete Figure 3 is reproduced below along with its unaltered legend. A revised Figure 6 and revised legend are reproduced on the next page.

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Figure 3. Intracellular localization of Dym-GFP in HeLa cells. (A) Reconstruction from 3D images of HeLa cells transfected with Dym-GFP and stained with antibodies against Giantin (in red, top line) and GalT (in blue, top line) or TGN46 (in red, bottom line) and GM130 (in blue, bottom line). Dym-GFP partially co-localized with the different Golgi markers and was also found as a soluble pool. (B) Immuno-gold labeling on cryosections of Dym-GFP transfected HeLa cells visualized by electron microscopy confirmed that the protein is localized on the Golgi apparatus and in the cytosol.
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Figure 6. Quantification of Dym-GFP dynamics. Hela cells were transfected with either Dym-GFP, Arf1-GFP or GRASP65-GFP and photobleaching experiments were performed 24 h after. (A) The Golgi apparatus of one cell (outlined in white in the movie) was bleached after 10 s and images were then acquired every 100 ms for 1 min (Supplementary Material, Movie 1). After 13.5 s the fluorescence of Dym-GFP has totally recovered. From these experiments we could quantify the Golgi fraction of the three proteins. The percentage of protein on the Golgi is represented in (B). 16.5 + 4% of Arf1-GFP, 13.6 + 3.9% of Dymeclin and 33.2 + 10.8% of GRASP65-GFP are on the Golgi. The normalized intensity of fluorescence for the three proteins was plotted on the same graph (C). The mean value is indicated in black and the SD is indicated in gray. The half-time of recovery was calculated from these data as shown in (D). GRASP65-GFP recovered more slowly with a half-time of 12.4 + 4.5 s, the recovery of Arf1-GFP was faster with a half-time of 7.1 + 2.6 s and Dym-GFP was even faster with a half-time of recovery of 2.8 + 0.9 s.
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