Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.

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.

Type

Journal article

Journal

FEBS Lett

Publication Date

09/12/1991

Volume

294

Pages

239 - 243

Keywords

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