通过与ADP-核糖基化因子1和RalA直接相互作用激活磷脂酶D1。
Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA.
作者信息
Kim J H, Lee S D, Han J M, Lee T G, Kim Y, Park J B, Lambeth J D, Suh P G, Ryu S H
机构信息
Department of Life Science and School of Environmental Engineering, Pohang University of Science and Technology, South Korea.
出版信息
FEBS Lett. 1998 Jul 3;430(3):231-5. doi: 10.1016/s0014-5793(98)00661-9.
Phospholipase D1 (PLD1) is known to be activated by ADP-ribosylation factor 1 (ARF1). We report here that ARF1 co-immunoprecipitates with PLD1 and that the ARF1-dependent PLD activation is induced by the direct interaction between ARF1 and PLD1. We found that RalA, another member of the small GTP-binding proteins, synergistically enhances the ARF1-dependent PLD activity with an EC50 of about 30 nM. Using in vitro binding assay, we show that ARF1 and RalA directly interact with different sites of PLD1. The results suggest that the independent interactions of RalA and ARF1 with PLD1 are responsible for the synergistic activation.
已知磷脂酶D1（PLD1）可被ADP-核糖基化因子1（ARF1）激活。我们在此报告，ARF1与PLD1发生共免疫沉淀，且ARF1依赖的PLD激活是由ARF1与PLD1之间的直接相互作用所诱导的。我们发现，小GTP结合蛋白的另一个成员RalA，以约30 nM的半数有效浓度（EC50）协同增强ARF1依赖的PLD活性。通过体外结合试验，我们表明ARF1和RalA直接与PLD1的不同位点相互作用。结果表明，RalA和ARF1与PLD1的独立相互作用导致了协同激活。
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