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Activation of phospholipase D1 by direct interaction with ADP‐ribosylation factor 1 and RalA
Author(s) -
Kim Jae Ho,
Lee Sang Do,
Han Jung Min,
Lee Taehoon G,
Kim Yong,
Park Jong Bae,
Lambeth J.David,
Suh Pann-Ghill,
Ryu Sung Ho
Publication year - 1998
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(98)00661-9
Subject(s) - adp ribosylation factor , adp ribosylation , chemistry , phospholipase , microbiology and biotechnology , phospholipase c , biophysics , biochemistry , signal transduction , biology , enzyme , endoplasmic reticulum , golgi apparatus , nad+ kinase
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 EC 50 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.