PLD2

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Protein-coding gene in the species Homo sapiens

title: "PLD2" type: doc version: 1 created: 2026-02-28 author: "Wikipedia contributors" status: active scope: public tags: ["ec-3.1.4"] description: "Protein-coding gene in the species Homo sapiens" topic_path: "general/ec-3-1-4" source: "https://en.wikipedia.org/wiki/PLD2" license: "CC BY-SA 4.0" wikipedia_page_id: 0 wikipedia_revision_id: 0

::summary Protein-coding gene in the species Homo sapiens ::

Phospholipase D2 is an enzyme that in humans is encoded by the PLD2 gene.

Function

Phosphatidylcholine (PC)-specific phospholipases D (PLDs) catalyze the hydrolysis of PC to produce phosphatidic acid and choline. Activation of PC-specific PLDs occurs as a consequence of agonist stimulation of both tyrosine kinase and G protein-coupled receptors. PC-specific PLDs have been proposed to function in regulated secretion, cytoskeletal reorganization, transcriptional regulation, and cell cycle control.[supplied by OMIM]

Mechanism of activation

PLD2 is activated by substrate presentation. The enzyme is palmitoylated, which drives PLD2 to lipid rafts. PC substrate is polyunsaturated and resides in the membrane separately from lipid rafts near phosphatidylinositol 4,5-bisphosphate (PIP2). When PIP2 levels increase, PLD2 trafficks to PIP2 where it encounters its substrate PC. Scaffolding proteins that interact with PLD2 likely changes its preference of lipid rafts vs PIP2.

Interactions

PLD2 has been shown to interact with:

Inhibitors

  • N-(2-(1-(3-fluorophenyl)-4-oxo-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)-2-naphthamide: 75-fold selective versus PLD1, IC50 = 20 nM.

References

References

  1. (February 1999). "Assignment of human PLD2 to chromosome band 17p13.1 by fluorescence in situ hybridization". Cytogenetics and Cell Genetics.
  2. (May 1998). "Cloning and initial characterization of a human phospholipase D2 (hPLD2). ADP-ribosylation factor regulates hPLD2". The Journal of Biological Chemistry.
  3. "Entrez Gene: PLD2 phospholipase D2".
  4. (December 2016). "Kinetic disruption of lipid rafts is a mechanosensor for phospholipase D". Nature Communications.
  5. (July 2001). "Actin directly interacts with phospholipase D, inhibiting its activity". The Journal of Biological Chemistry.
  6. (July 2000). "Cardiac phospholipase D2 localizes to sarcolemmal membranes and is inhibited by alpha-actinin in an ADP-ribosylation factor-reversible manner". The Journal of Biological Chemistry.
  7. (March 2002). "Phospholipase D2 directly interacts with aldolase via Its PH domain". Biochemistry.
  8. (June 2000). "Inhibition of phospholipase D by amphiphysins". The Journal of Biological Chemistry.
  9. (December 2003). "Aquaporin 3 colocates with phospholipase d2 in caveolin-rich membrane microdomains and is downregulated upon keratinocyte differentiation". The Journal of Investigative Dermatology.
  10. (February 2000). "Phospholipase D2: functional interaction with caveolin in low-density membrane microdomains". FEBS Letters.
  11. (June 2003). "Hydrogen peroxide induces association between glyceraldehyde 3-phosphate dehydrogenase and phospholipase D2 to facilitate phospholipase D2 activation in PC12 cells". Journal of Neurochemistry.
  12. (May 2003). "The direct interaction of phospholipase C-gamma 1 with phospholipase D2 is important for epidermal growth factor signaling". The Journal of Biological Chemistry.
  13. (March 2002). "Phosphorylation-dependent regulation of phospholipase D2 by protein kinase C delta in rat Pheochromocytoma PC12 cells". The Journal of Biological Chemistry.
  14. (May 2003). "Transmodulation between phospholipase D and c-Src enhances cell proliferation". Molecular and Cellular Biology.
  15. (November 2011). "A novel phospholipase D2-Grb2-WASp heterotrimer regulates leukocyte phagocytosis in a two-step mechanism". Molecular and Cellular Biology.
  16. (September 2010). "Design, synthesis, and biological evaluation of halogenated N-(2-(4-oxo-1-phenyl-1,3,8-triazaspiro[4.5]decan-8-yl)ethyl)benzamides: discovery of an isoform-selective small molecule phospholipase D2 inhibitor". Journal of Medicinal Chemistry.

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