| Publication type: | Article in scientific journal |
| Type of review: | Peer review (publication) |
| Title: | Transition of galactosyltransferase 1 from trans-golgi cisterna to the trans-golgi network is signal mediated |
| Authors: | Schaub, Beat E. Berger, Bea Berger, Eric G. Rohrer, Jack |
| DOI: | 10.1091/mbc.e06-08-0665 |
| Published in: | Molecular Biology of the Cell |
| Volume(Issue): | 17 |
| Issue: | 12 |
| Page(s): | 5153 |
| Pages to: | 5162 |
| Issue Date: | Dec-2006 |
| Publisher / Ed. Institution: | American Society for Cell Biology |
| ISSN: | 1939-4586 1059-1524 |
| Language: | English |
| Subject (DDC): | 571: Physiology and related subjects |
| Abstract: | The Golgi apparatus (GA) is the organelle where complex glycan formation takes place. In addition, it is a major sorting site for proteins destined for various subcellular compartments or for secretion. Here we investigate beta1,4-galactosyltransferase 1 (galT) and alpha2,6-sialyltransferase 1 (siaT), two trans-Golgi glycosyltransferases, with respect to their different pathways in monensin-treated cells. Upon addition of monensin galT dissociates from siaT and the GA and accumulates in swollen vesicles derived from the trans-Golgi network (TGN), as shown by colocalization with TGN46, a specific TGN marker. We analyzed various chimeric constructs of galT and siaT by confocal fluorescence microscopy and time-lapse videomicroscopy as well as Optiprep density gradient fractionation. We show that the first 13 amino acids of the cytoplasmic tail of galT are necessary for its localization to swollen vesicles induced by monensin. We also show that the monensin sensitivity resulting from the cytoplasmic tail can be conferred to siaT, which leads to the rapid accumulation of the galT-siaT chimera in swollen vesicles upon monensin treatment. On the basis of these data, we suggest that cycling between the trans-Golgi cisterna and the trans-Golgi network of galT is signal mediated. |
| URI: | https://digitalcollection.zhaw.ch/handle/11475/6806 |
| Fulltext version: | Published version |
| License (according to publishing contract): | Licence according to publishing contract |
| Departement: | Life Sciences and Facility Management |
| Organisational Unit: | Institute of Chemistry and Biotechnology (ICBT) |
| Appears in collections: | Publikationen Life Sciences und Facility Management |
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Schaub, B. E., Berger, B., Berger, E. G., & Rohrer, J. (2006). Transition of galactosyltransferase 1 from trans-golgi cisterna to the trans-golgi network is signal mediated. Molecular Biology of the Cell, 17(12), 5153–5162. https://doi.org/10.1091/mbc.e06-08-0665
Schaub, B.E. et al. (2006) ‘Transition of galactosyltransferase 1 from trans-golgi cisterna to the trans-golgi network is signal mediated’, Molecular Biology of the Cell, 17(12), pp. 5153–5162. Available at: https://doi.org/10.1091/mbc.e06-08-0665.
B. E. Schaub, B. Berger, E. G. Berger, and J. Rohrer, “Transition of galactosyltransferase 1 from trans-golgi cisterna to the trans-golgi network is signal mediated,” Molecular Biology of the Cell, vol. 17, no. 12, pp. 5153–5162, Dec. 2006, doi: 10.1091/mbc.e06-08-0665.
SCHAUB, Beat E., Bea BERGER, Eric G. BERGER und Jack ROHRER, 2006. Transition of galactosyltransferase 1 from trans-golgi cisterna to the trans-golgi network is signal mediated. Molecular Biology of the Cell. Dezember 2006. Bd. 17, Nr. 12, S. 5153–5162. DOI 10.1091/mbc.e06-08-0665
Schaub, Beat E., Bea Berger, Eric G. Berger, and Jack Rohrer. 2006. “Transition of Galactosyltransferase 1 from Trans-Golgi Cisterna to the Trans-Golgi Network Is Signal Mediated.” Molecular Biology of the Cell 17 (12): 5153–62. https://doi.org/10.1091/mbc.e06-08-0665.
Schaub, Beat E., et al. “Transition of Galactosyltransferase 1 from Trans-Golgi Cisterna to the Trans-Golgi Network Is Signal Mediated.” Molecular Biology of the Cell, vol. 17, no. 12, Dec. 2006, pp. 5153–62, https://doi.org/10.1091/mbc.e06-08-0665.
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