Activation of phospholipase D1 by direct interaction with ADP-ribosylation factor 1 and RalA.
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.
Department of Life Science and School of Environmental Engineering, Pohang University of Science and Technology, South Korea.
J H
JH
Kim
S D
SD
Lee
J M
JM
Han
T G
TG
Lee
Y
Y
Kim
J B
JB
Park
J D
JD
Lambeth
P G
PG
Suh
S H
SH
Ryu
D020823:ADP-Ribosylation Factor 1; D020727:ADP-Ribosylation Factors; D000818:Animals; D002417:Cattle; D004789:Enzyme Activation; D019204:GTP-Binding Proteins / Q000378:metabolism*; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism; D010739:Phospholipase D / Q000378:metabolism*; D011233:Precipitin Tests; D011485:Protein Binding; D011993:Recombinant Fusion Proteins; D020725:ral GTP-Binding Proteins
D019269:Phosphatidylinositol 4,5-Diphosphate; D011993:Recombinant Fusion Proteins; D010739:Phospholipase D; C106801:phospholipase D1; D019204:GTP-Binding Proteins; D020823:ADP-Ribosylation Factor 1; D020727:ADP-Ribosylation Factors; D020725:ral GTP-Binding Proteins