Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA

被引：84

作者：

Kim, JH

Lee, SD

Han, JM

Lee, TG

Kim, Y

Park, JB

Lambeth, JD

Suh, PG

Ryu, SH ^{[1
]}

机构：

[1] Pohang Univ Sci & Technol, Dept Life Sci, Pohang 790784, South Korea

[2] Pohang Univ Sci & Technol, Sch Environm Engn, Pohang 790784, South Korea

[3] Emory Univ, Sch Med, Dept Biochem, Atlanta, GA 30322 USA

来源：

FEBS LETTERS | 1998年 / 430卷 / 03期

关键词：

phospholipase D1; adenosine diphosphate-ribosylation factor 1; RalA; phosphatidylinositol 4,5-bisphosphate;

D O I：

10.1016/S0014-5793(98)00661-9

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 hv 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, (C) 1998 Federation of European Biochemical Societies.

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收藏

页码：231 / 235

页数：5

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