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A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network
Author(s) -
Barr Francis A.,
Huttner Wieland B.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00285-2
Subject(s) - adp ribosylation factor , golgi apparatus , biogenesis , microbiology and biotechnology , vesicle , chemistry , secretory vesicle , copi , secretory pathway , biophysics , biology , biochemistry , endoplasmic reticulum , gene , membrane
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.