FEBS Letters | |
Arfaptin 1 forms a complex with ADP‐ribosylation factor and inhibits phospholipase D | |
Provost, J.J1  Ho, W.-T1  Williger, B.-T1  Exton, J.H1  Milstine, J1  | |
[1] Howard Hughes Medical Institute and Department of Molecular Physiology and Biophysics, Vanderbilt University School of Medicine, Nashville, TN 37232-0295, USA | |
关键词: ADP-ribosylation factor; Arfaprin; Phospholipase D inhibition; ARF; ADP-ribosylation factor; ATP; adenosine triphosphate; BSA; bovine serum albumin; GDPβS; guanosine-5′-O-(2-thiodiphosphate); GTPγS; guanosine-5′-O-(3-thiotriphosphate); PBS; phosphate-buffered saline; DMEM; Dulbecco's modified Eagle's medium; myrARF3; myristoylated ARF3; PKC; protein kinase C; PLD; phospholipase D; GST; glutathione S-transferase; | |
DOI : 10.1016/S0014-5793(99)00771-1 | |
学科分类:生物化学/生物物理 | |
来源: John Wiley & Sons Ltd. | |
【 摘 要 】
ADP-ribosylation factors (ARFs) regulate coatomer assembly on the Golgi as well as recruitment of clathrin adapter proteins and are therefore involved in vesicle budding from the Golgi and vesicular transport. They are also regulators of phospholipase D (PLD) activity. Arfaptin 1 is an ARF binding protein that inhibits PLD activation, vesicular trafficking and secretion. In the present report, we show that arfaptin 1 interacts with ‘high speed’ membranes independently of ARF. However, addition of myristoylated ARF3 (myrARF3) increases the association of arfaptin 1 with the membranes, suggesting that arfaptin 1 and ARF form a complex on the Golgi. Utilizing several deletion mutants of arfaptin 1 it is shown that the association of arfaptin 1 with myrARF3 is mediated via two binding sites on arfaptin 1. These two domains are needed for arfaptin 1 inhibition of PLD activation by myrARF3 in vitro.
【 授权许可】
Unknown
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