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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Corda, D. Colanzi, A. Di Tullio, G. Fusella, A. Luini, A. Silletta, M. G. Mironov, A. Fiucci, G. Polishchuk, R. Malhotra, V. De Matteis, M. A. Weigert, R. Flati, S. |
| Description | Author Affiliation: Mironov A ( Department of Cell Biology and Oncology, Istituto di Ricerche Farmacologiche Mario Negri, Consorzio Mario Negri Sud, 66030 Santa Maria Imbaro (Chieti), Italy. mironov@cmns.mnegri.it) |
| Abstract | We have investigated the role of the ADP- ribosylation induced by brefeldin A (BFA) in the mechanisms controlling the architecture of the Golgi complex. BFA causes the rapid disassembly of this organelle into a network of tubules, prevents the association of coatomer and other proteins to Golgi membranes, and stimulates the ADP-ribosylation of two cytosolic proteins of 38 and 50 kD (GAPDH and BARS-50; De Matteis, M.A., M. DiGirolamo, A. Colanzi, M. Pallas, G. Di Tullio, L.J. McDonald, J. Moss, G. Santini, S. Bannykh, D. Corda, and A. Luini. 1994. Proc. Natl. Acad. Sci. USA. 91:1114–1118; Di Girolamo, M., M.G. Silletta, M.A. De Matteis, A. Braca, A. Colanzi, D. Pawlak, M.M. Rasenick, A. Luini, and D. Corda. 1995. Proc. Natl. Acad. Sci. USA. 92:7065–7069). To study the role of ADP-ribosylation, this reaction was inhibited by depletion of $NAD^{+}$ (the ADP-ribose donor) or by using selective pharmacological blockers in permeabilized cells. In $NAD^{+}-depleted$ cells and in the presence of dialized cytosol, BFA detached coat proteins from Golgi membranes with normal potency but failed to alter the organelle's structure. Readdition of $NAD^{+}$ triggered Golgi disassembly by BFA. This effect of $NAD^{+}$ was mimicked by the use of pre–ADP- ribosylated cytosol. The further addition of extracts enriched in native BARS-50 abolished the ability of ADP-ribosylated cytosol to support the effect of BFA. Pharmacological blockers of the BFA-dependent ADP-ribosylation (Weigert, R., A. Colanzi, A. Mironov, R. Buccione, C. Cericola, M.G. Sciulli, G. Santini, S. Flati, A. Fusella, J. Donaldson, M. DiGirolamo, D. Corda, M.A. De Matteis, and A. Luini. 1997. J. Biol. Chem. 272:14200–14207) prevented Golgi disassembly by BFA in permeabilized cells. These inhibitors became inactive in the presence of pre–ADP-ribosylated cytosol, and their activity was rescued by supplementing the cytosol with a native BARS-50–enriched fraction. These results indicate that ADP-ribosylation plays a role in the Golgi disassembling activity of BFA, and suggest that the ADP-ribosylated substrates are components of the machinery controlling the structure of the Golgi apparatus. |
| ISSN | 00219525 |
| e-ISSN | 15408140 |
| Journal | The Journal of Cell Biology |
| Issue Number | 5 |
| Volume Number | 139 |
| Language | English |
| Publisher | Rockefeller University Press (United States) |
| Publisher Date | 1997-12-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Adenosine Diphosphate Ribose Metabolism Cyclopentanes Pharmacology Golgi Apparatus Ultrastructure NAD Animals Brefeldin A Cell Membrane Permeability Coatomer Protein Endoplasmic Reticulum Enzymology Drug Effects Membrane Proteins Tumor Cells, Cultured Research Support, Non-U.S. Gov't Cell Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Medicine |
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