Powner Dale J, Wakelam Michael J O
CR UK Institute for Cancer Studies, Birmingham University, B15 2TT, Birmingham, UK.
FEBS Lett. 2002 Oct 30;531(1):62-4. doi: 10.1016/s0014-5793(02)03410-5.
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.
磷脂酶D1和D2（PLD1、PLD2）在其N端区域均具有PX和PH结构域，这些肌醇脂质结合结构域在调节PLD活性和定位中起关键作用。PLD1的活性还受蛋白激酶C以及Rho和Arf家族小GTP酶成员的调节。这些蛋白质中的每一种都与独特的位点结合；然而，在体外似乎很难区分各个家族成员。然而，在激动剂刺激的细胞中存在特异性，例如在RBL-2H3细胞中，抗原通过与Arf6、Rac1和蛋白激酶Cα结合来刺激PLD1的激活。PLD2似乎较少直接受小GTP酶的调节，而是主要通过与生成激活磷脂酰肌醇4,5-二磷酸的磷脂酰肌醇4-磷酸5-激酶相互作用来控制。
