A role for ADP‐ribosylation factor 1, but not COP I, in secretory vesicle biogenesis from the trans‐Golgi network

FEBS Letters

Huttner, Wieland B.¹  Barr, Francis A.¹ 

[1] Cell Biology Programme, European Molecular Biology Laboratory, Meyerhofstraβe 1, D-69120 Heidelberg, Germany

关键词: Budding;    Coatomer;    Fission;    Phospholipase D;    ARF;    ADP-ribosylation factor;    CSVs;    constitutive secretory vesicles;    ISGs;    immature secretory granules;    PNS;    postnuclear supernatant;    TGN;    trans-Golgi network;   

DOI  :  10.1016/0014-5793(96)00285-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown