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Human ADP-ribosylation Factor-activated Phosphatidylcholine-specific Phospholipase D Defines a New and Highly Conserved Gene Family
Open accessAbstract
Activation of phosphatidylcholine-specific phospholipase D (PLD) has been implicated as a critical step in numerous cellular pathways, including signal transduction, membrane trafficking, and the regulation of mitosis. We report here the identification of the first human PLD cDNA, which defines a new and highly conserved gene family. Characterization of recombinant human PLD1 reveals that it is membrane-associated, selective for phosphatidylcholine, stimulated by phosphatidylinositol 4,5-bisphosphate, activated by the monomeric G-protein ADP-ribosylation factor-1, and inhibited by oleate. PLD1 likely encodes the gene product responsible for the most widely studied endogenous PLD activity.
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Cited by
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Zhang, Y., Liu, X., Bai, J., Tian, X., Zhao, X., Liu, W., Duan, X., Shang, W., Fan, H.-Y., & Tong, C. (2016) · Molecular Cell · doi:10.1016/j.molcel.2015.11.017 · Cited by 145
Enzymological studies on the biosynthesis of N-acylethanolamines
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Metadata
- Authors
- Hammond, S. M., Altshuller, Y. M., Sung, T.-C., Rudge, S. A., Rose, K., Engebrecht, J., Morris, A. J., & Frohman, M. A.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1995-12
- Volume
- 270
- Issue
- 50
- Pages
- 29640-29643
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2085391208
- Cited by
- 658
- References
- 0
- FWCI
- 18.71
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- CoChat. (2026). Citation check: Human ADP-ribosylation Factor-activated Phosphatidylcholine-specific Phospholipase D Defines a New and Highly Conserved Gene Family. https://app.cochat.ai/papers/10.1074/jbc.270.50.29640
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- Hammond, S. M., Altshuller, Y. M., Sung, T.-C., Rudge, S. A., Rose, K., Engebrecht, J., Morris, A. J., & Frohman, M. A. (1995). Human ADP-ribosylation Factor-activated Phosphatidylcholine-specific Phospholipase D Defines a New and Highly Conserved Gene Family. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.270.50.29640
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