Abstract
New Insights into Phospholipase D and Sphingosine Kinase Activation in Arabidopsis
Highlights
Work from the Wang laboratory showed that the two tonoplastic SPHK1 and SPHK2 isoenzymes from Arabidopsis thaliana can be activated by phospholipase D α1 (PLDα1)-derived phosphatidic acid (PA) species, and that sphingosine kinase (SPHK)-derived phytosphingosine-1-phosphate acts upstream of PLDα1
This is supported by the observation that diacylglycerol, which is structurally similar to PA but lacking the phosphate group did not activate SPHKs (Olivera et al, 1996)
The situation appears to differ in the case of A. thaliana SPHK1 and SPHK2 as these enzymes do not appear to interact with other phospholipids such as phosphatidylcholine, phosphatidylethanolamine, phosphatidylglycerol, phosphatidylinositol, phosphatidylserine, lysophosphatidylcholine, and lysophosphatidylethanolamine (Guo et al, 2011)
Summary
Work from the Wang laboratory showed that the two tonoplastic SPHK1 and SPHK2 isoenzymes from Arabidopsis thaliana can be activated by phospholipase D α1 (PLDα1)-derived phosphatidic acid (PA) species, and that SPHK-derived phytosphingosine-1-phosphate (phyto-S1P) acts upstream of PLDα1 (see this review by Guo and Wang). Guo and Wang have provided a comprehensive review of the crosstalk between the sphingolipid and phospholipid pathways and their potential roles in regulating signaling processes.
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