Journal
EMBO JOURNAL
Volume 28, Issue 9, Pages 1197-1207Publisher
WILEY
DOI: 10.1038/emboj.2009.78
Keywords
CtBP1/BARS; macropinocytosis; phospholipase D
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Funding
- Ministry of Education, Science, Sports and Culture of Japan
- Bilateral Exchange Program between Japan Society for the Promotion of Science and Polish Academy of Sciences
- Osaka Medical Research Foundation for Incurable Diseases
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Vesicular trafficking such as macropinocytosis is a dynamic process that requires coordinated interactions between specialized proteins and lipids. A recent report suggests the involvement of CtBP1/BARS in epidermal growth factor (EGF)-induced macropinocytosis. Detailed mechanisms as to how lipid remodelling is regulated during macropinocytosis are still undefined. Here, we show that CtBP1/BARS is a physiological activator of PLD1 required in agonist-induced macropinocytosis. EGF-induced macropinocytosis was specifically blocked by 1-butanol but not by 2-butanol. In addition, stimulation of cells by serum or EGF resulted in the association of CtBP1/BARS with PLD1. Finally, CtBP1/BARS activated PLD1 in a synergistic manner with other PLD activators, including ADP-ribosylation factors as demonstrated by in vitro and intact cell systems. The present results shed light on the molecular basis of how the 'fission protein' CtBP1/BARS controls vesicular trafficking events including macropinocytosis. The EMBO Journal (2009) 28, 1197-1207. doi: 10.1038/emboj.2009.78; Published online 26 March 2009
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