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Suh, Pann-Ghill
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Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA

Author(s)
Kim, Jae HoLee, Sang DoHan, Jung MinLee, Taehoon GKim, YongPark, Jong BaeLambeth, J. DavidSuh, Pann-GhillRyu, Sung Ho
Issued Date
1998-07
DOI
10.1016/S0014-5793(98)00661-9
URI
https://scholarworks.unist.ac.kr/handle/201301/18533
Fulltext
http://www.sciencedirect.com/science/article/pii/S0014579398006619
Citation
FEBS LETTERS, v.430, no.3, pp.231 - 235
Abstract
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
Publisher
ELSEVIER SCIENCE BV
ISSN
0014-5793

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