CtBP1/BARS is an activator of phospholipase D1 necessary for agonist-induced macropinocytosis

• Yuki Haga ^[1] ; Noriko Miwa ^[1] ; Saleem Jahangeer ^[1] ; Taro Okada ^[1] ; Shun-ichi Nakamura ^[1]
  1. [1] Kobe University

     Kobe University

     Chuo-ku, Japón

     
• Localización: EMBO journal: European Molecular Biology Organization, ISSN 0261-4189, Vol. 28, Nº. 9, 2009, págs. 1197-1207
• Idioma: inglés
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• Resumen

  • 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.