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Non-hydrolysable analogues of GTP, such as GTP gamma S and GMP-PNP, have previously been shown to inhibit the formation of constitutive secretory vesicles (CSVs) and immature secretory granules (ISGs) from the trans-Golgi network (TGN). Using a cell-free system, we show here that the formation of these vesicles is also inhibited by [A1F4]-, a compound known to act on trimeric G-proteins. Addition of highly purified G-protein beta gamma subunits stimulated, in a differential manner, the cell-free formation of both CSVs and ISGs. ADP-ribosylation experiments revealed the presence of a pertussis toxin-sensitive G-protein alpha subunit in the TGN. We conclude that trimeric G-proteins regulate the formation of secretory vesicles from the TGN.


Journal article



Publication Date





239 - 243


Adenosine Diphosphate Ribose, Adrenal Gland Neoplasms, Aluminum, Aluminum Compounds, Cell-Free System, Cytoplasmic Granules, Fluorides, GTP-Binding Proteins, Golgi Apparatus, Macromolecular Substances, Pertussis Toxin, Pheochromocytoma, Tumor Cells, Cultured, Virulence Factors, Bordetella