The regulation of phospholipase D by inosital phospholipids and small GTPases

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Colleges, School and Institutes


Phospholipase D1 and D2 (PLD1, PLD2) both have PX and PH domains in their N-terminal regions with these inositol lipid binding domains playing key roles in regulating PLD activity and localisation. The activity of PLD1 is also regulated by protein kinase C and members of the Rho and Arf families of GTPases. Each of these proteins binds to unique sites; however, there appears to be little in vitro discrimination between individual family members. In agonist-stimulated cells, however, there is specificity, with, for example in RBL-2H3 cells, antigen stimulating the activation of PLD1 by association with Arf6, Rac1 and protein kinase Calpha. PLD2 appears to be less directly regulated by GTPases and rather is primarily controlled through interaction with phosphatidylinositol 4-phosphate 5-kinase that generates the activating phosphatidylinositol, 4,5-bisphosphate. (C) 2002 Published by Elsevier Science B.V. on behalf of the Federation of European Biochemical Societies.


Original languageEnglish
Pages (from-to)62-64
Number of pages3
JournalFEBS Letters
Issue number1
Publication statusPublished - 1 Oct 2002


  • Rac1, phospholipase D, phosphatidylinositol 4-phosphate 5-kinase, phosphatidylinositol 4,5-bisphosphate, Arf6