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A synthetic N-myristoylated peptide corresponding to the amino-terminal domain of ADP-ribosylation factor 1 (ARF1) markedly increases, in a cell-free system using post-nuclear supernatant from PC12 cells, the biogenesis of constitutive secretory vesicles and immature secretory granules from the trans-Golgi network (TGN). The related N-myristoylated ARF4 peptide only weakly stimulates, and the non-myristoylated ARF1 and ARF4 peptides inhibit, the biogenesis of these secretory vesicles. In a modified cell-free system using TGN membranes, coatomer-depleted cytosol supports the biogenesis of TGN-derived secretory vesicles to the same extent as control cytosol. These results suggest a role for ARF1, but not the COP I coat, in secretory vesicle biogenesis from the TGN, possibly via the activation of phospholipase D.

Type

Journal article

Journal

FEBS Lett

Publication Date

08/04/1996

Volume

384

Pages

65 - 70

Keywords

ADP-Ribosylation Factor 1, ADP-Ribosylation Factors, Adenosine Triphosphate, Animals, Arabidopsis Proteins, Carrier Proteins, Cell-Free System, Cytoplasmic Granules, Cytosol, GTP-Binding Proteins, Golgi Apparatus, Guanosine 5'-O-(3-Thiotriphosphate), Intracellular Membranes, Kinetics, Myristic Acid, Myristic Acids, PC12 Cells, Plant Proteins, Rats, Sulfates, Sulfur Radioisotopes, Ubiquitin-Protein Ligases