Cookies on this website

We use cookies to ensure that we give you the best experience on our website. If you click 'Accept all cookies' we'll assume that you are happy to receive all cookies and you won't see this message again. If you click 'Reject all non-essential cookies' only necessary cookies providing core functionality such as security, network management, and accessibility will be enabled. Click 'Find out more' for information on how to change your cookie settings.

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.


Journal article



Publication Date





65 - 70


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