Cellular and Molecular Life Sciences CMLS

, Volume 58, Issue 11, pp 1674–1687

Signalling roles of mammalian phospholipase D1 and D2

  • S. Cockcroft

DOI: 10.1007/PL00000805

Cite this article as:
Cockcroft, S. CMLS, Cell. Mol. Life Sci. (2001) 58: 1674. doi:10.1007/PL00000805


Phospholipase D (PLD) catalyses the hydrolysis of phosphatidylcholine to generate the lipid second messenger, phosphatidate (PA) and choline. PLD activity in mammalian cells is low and is transiently stimulated upon activation by G-protein-coupled and receptor tyrosine kinase cell surface receptors. Two mammalian PLD enzymes (PLD1 and PLD2) have been cloned and their intracellular regulators identified as ARF and Rho proteins, protein kinase Cα as well as the lipid, phosphatidylinositol [4, 5] bisphosphate (PIP2). I discuss the regulation of these enzymes by cell surface receptors, their cellular localisation and the potential function of PA as a second messenger. Evidence is presented for a role of PA in regulating the lipid kinase activity of PIP 5-kinase, an enzyme that synthesises PIP2. A signalling role of phospholipase D via PA and indirectly via PIP2 in regulating membrane traffic and actin dynamics is indicated by the available data.

Key words. Phospholipase D; ADP ribosylation factor; Rho protein; phosphatidic acid; phosphatidylinositol(4,5)bisphosphate. 

Copyright information

© Birkhäuser Verlag, 2001

Authors and Affiliations

  • S. Cockcroft
    • 1
  1. 1.Department of Physiology, Rockefeller Building, University College London, University St., London WC1E 6JJ (United Kingdom), Fax: + 44 71 387 6368, e-mail: ucgbsxc@ucl.ac.ukGB

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