Antonny B, Huber I, Paris S, Chabre M, Cassel D
CNRS, Institut de Pharmacologie Moléculaire et Cellulaire, 660 route des lucioles, 06560 Valbonne, France.
J Biol Chem. 1997 Dec 5;272(49):30848-51. doi: 10.1074/jbc.272.49.30848.
Disassembly of the coatomer from Golgi vesicles requires that the small GTP-binding protein ADP-ribosylation factor 1 (ARF1) hydrolyzes its bound GTP by the action of a GTPase-activating protein. In vitro, the binding of the ARF1 GTPase-activating protein to lipid vesicles and its activity on membrane-bound ARF1GTP are increased by diacylglycerols with monounsaturated acyl chains, such as those arising in vivo as secondary products from the hydrolysis of phosphatidylcholine by ARF-activated phospholipase D. Thus, the phospholipase D pathway may provide a feedback mechanism that promotes GTP hydrolysis on ARF1 and the consequent uncoating of vesicles.
从高尔基体囊泡上拆卸包被蛋白需要小GTP结合蛋白ADP核糖基化因子1（ARF1）通过GTP酶激活蛋白的作用水解其结合的GTP。在体外，ARF1 GTP酶激活蛋白与脂质囊泡的结合及其对膜结合的ARF1GTP的活性会因具有单不饱和酰基链的二酰基甘油而增加，例如体内由ARF激活的磷脂酶D水解磷脂酰胆碱产生的次级产物。因此，磷脂酶D途径可能提供一种反馈机制，促进ARF1上的GTP水解以及随后囊泡的脱包被。
