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The regulation of phospholipase D by inositol phospholipids and small GTPases
Author(s) -
Powner Dale J,
Wakelam Michael J.O
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)03410-5
Subject(s) - inositol , gtpase , phospholipase c , phospholipase , phospholipase d , chemistry , microbiology and biotechnology , gq alpha subunit , biochemistry , biology , g protein , signal transduction , receptor , enzyme
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 Cα. 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.