Human Molecular Genetics 2009, 18 (3):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.

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.

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.

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.

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.