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CtBP1/BARS is an activator of phospholipase D1 necessary for agonist‐induced macropinocytosis
Author(s) -
Haga Yuki,
Miwa Noriko,
Jahangeer Saleem,
Okada Taro,
Nakamura Shunichi
Publication year - 2009
Publication title -
the embo journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.484
H-Index - 392
eISSN - 1460-2075
pISSN - 0261-4189
DOI - 10.1038/emboj.2009.78
Subject(s) - biology , pinocytosis , agonist , activator (genetics) , microbiology and biotechnology , phospholipase c , endocrinology , receptor , biochemistry , signal transduction , endocytosis
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.