Regular ArticleRalA Interacts Directly with the Arf-Responsive, PIP2-Dependent Phospholipase D1☆
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Structure and regulation of human phospholipase D
2021, Advances in Biological RegulationCitation Excerpt :The precipitated PLD was PI(4,5)P2 dependent and Arf1/3 stimulated, and was confirmed to be PLD1 using PLD1 specific antibodies(Kim, 1998; Luo et al., 1997). RalA D49N increased PLD1 precipitation, while deletion of the initial eleven RalA residues strongly reduced interaction(Jiang et al., 1995a,b; Luo et al., 1997). Purified RalA is unable to precipitate purified PLD2, which suggests there is no interaction(Luo et al., 1997).
Mammalian phospholipase D: Function, and therapeutics
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2011, Journal of Biological ChemistryCitation Excerpt :These data are consistent with RalA being a key target of nutrients for the activation of mTORC1 and further implicate PLD1, which interacts directly with RalA as a conduit to mTORC1 activation. We previously reported that RalA promotes the activation of PLD1 by recruitment of ARF family GTPases into a RalA-PLD1 complex (14, 18). We also demonstrated that H-Ras-induced PLD activity was dependent on ARF6 (40).
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DG, diacylglycerolPEt, phosphatidylethanol; PA, phosphatidic acid; PC, phosphatidylcholine; PIP2, phosphatidylinositol-4,5-bisphosphate; PLD, phospholipase D;
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Present address: The Rockefeller University, New York, NY 10021.
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To whom correspondence should be addressed at the Department of Biological Sciences, Hunter College of The City University of New York, 695 Park Avenue, New York, NY 10021. Fax: (212) 772-5227. E-mail: [email protected].