Dissociation of Coatomer from Membranes Is Required for Brefeldin A–induced Transfer of Golgi Enzymes to the Endoplasmic Reticulum
| Autor: | Gareth Griffiths, Rainer Pepperkok, Thomas E. Kreis, Jochen Scheel, Martin Lowe |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 1997 |
| Předmět: |
Microinjections
Receptors Peptide KDEL Golgi Apparatus Cyclopentanes Biology Endoplasmic Reticulum Coatomer Protein Article Antibodies Vesicular stomatitis Indiana virus 03 medical and health sciences chemistry.chemical_compound symbols.namesake 0302 clinical medicine Viral Envelope Proteins Chlorocebus aethiops Animals Vero Cells Secretory pathway 030304 developmental biology Protein Synthesis Inhibitors 0303 health sciences Golgi membrane Brefeldin A Membrane Glycoproteins Vesicular-tubular cluster Endoplasmic reticulum Biological Transport Cell Biology COPI Intracellular Membranes Golgi apparatus Cell biology chemistry symbols Peptides Microtubule-Associated Proteins 030217 neurology & neurosurgery Biomarkers |
| Zdroj: | The Journal of Cell Biology |
| ISSN: | 1540-8140 0021-9525 |
| Popis: | Addition of brefeldin A (BFA) to mammalian cells rapidly results in the removal of coatomer from membranes and subsequent delivery of Golgi enzymes to the endoplasmic reticulum (ER). Microinjected anti-EAGE (intact IgG or Fab-fragments), antibodies against the "EAGE"-peptide of beta-COP, inhibit BFA-induced redistribution of beta-COP in vivo and block transfer of resident proteins of the Golgi complex to the ER; tubulo-vesicular clusters accumulate and Golgi membrane proteins concentrate in cytoplasmic patches containing beta-COP. These patches are devoid of marker proteins of the ER, the intermediate compartment (IC), and do not contain KDEL receptor. Interestingly, relocation of KDEL receptor to the IC, where it colocalizes with ERGIC53 and ts-O45-G, is not inhibited under these conditions. While no stacked Golgi cisternae remain in these injected cells, reassembly of stacks of Golgi cisternae following BFA wash-out is inhibited to only approximately 50%. Mono- or divalent anti-EAGE stabilize binding of coatomer to membranes in vitro, at least as efficiently as GTP(gamma)S. Taken together these results suggest that enhanced binding of coatomer to membranes completely inhibits the BFA-induced retrograde transport of Golgi resident proteins to the ER, probably by inhibiting fusion of Golgi with ER membranes, but does not interfere with the disassembly of the stacked Golgi cisternae and recycling of KDEL receptor to the IC. These results confirm our previous results suggesting that COPI is involved in anterograde membrane transport from the ER/IC to the Golgi complex (Pepperkok et al., 1993), and corroborate that COPI regulates retrograde membrane transport between the Golgi complex and ER in mammalian cells. |
| Databáze: | OpenAIRE |
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