Trimeric G-proteins of the trans-Golgi network are involved in the formation of constitutive secretory vesicles and immature secretory granules

FEBS Lett. 1991 Dec 9;294(3):239-43. doi: 10.1016/0014-5793(91)81438-e.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Adenosine Diphosphate Ribose / metabolism
  • Adrenal Gland Neoplasms
  • Aluminum / pharmacology
  • Aluminum Compounds*
  • Cell-Free System
  • Cytoplasmic Granules / physiology*
  • Fluorides / pharmacology
  • GTP-Binding Proteins / antagonists & inhibitors
  • GTP-Binding Proteins / chemistry
  • GTP-Binding Proteins / physiology*
  • Golgi Apparatus / chemistry*
  • Golgi Apparatus / ultrastructure
  • Macromolecular Substances
  • Pertussis Toxin
  • Pheochromocytoma
  • Tumor Cells, Cultured
  • Virulence Factors, Bordetella / pharmacology

Substances

  • Aluminum Compounds
  • Macromolecular Substances
  • Virulence Factors, Bordetella
  • Adenosine Diphosphate Ribose
  • Aluminum
  • Pertussis Toxin
  • GTP-Binding Proteins
  • Fluorides
  • aluminum fluoride