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Papers In Press, published online ahead of print July 16, 2007
Biochemistry and Molecular Biology, Uniformed Services University of the Health Sciences, Bethesda, MD 20814
Corresponding Author: tdunn{at}usuhs.mil
The sphingoid long chain bases (LCBs) and their phosphorylated derivatives (LCB-Ps) are important signalling molecules in eu-karyotic organisms. The cellular levels of LCB-Ps are tightly controlled by the coordi-nated action of the LCB kinase activity re-sponsible for their synthesis and the LCB-P phosphatase and lyase activities responsible for their catabolism. Although recent stud-ies have implicated LCB-Ps as regulatory molecules in plants, in comparison to yeast and mammals, much less is known about their metabolism and function in plants. To investigate the functions of LCB-Ps in plants, we have undertaken the identification and characterization of Arabidopsis genes that encode the enzymes of LCB-P metabolism. In this study the Arabidopsis At1g27980 gene, was shown to encode the only detectable LCB-P lyase activity in Arabidopsis. The LCB-P lyase activity was characterized and mutant plant lines lacking the lyase were generated and analyzed. Whereas in other organisms loss of LCB-P lyase activity is associated with accumulation of high levels of LCB/LCB-Ps and developmental abnormalities, the sphingolipid profiles of the mutant plants were remarka-bly similar to those of wild-type plants and no developmental abnormalities were observed. Thus, these studies indicate that the lyase plays a minor role in maintenance of sphingolipid metabolism during normal plant development and growth. However, a clear role for the lyase was revealed upon perturbation of sphingolipid synthesis by treatment with the inhibitor of ceramide synthase, fumonisin B1.
J. Biol. Chem, 10.1074/jbc.M705074200
Submitted on June 20, 2007
Revised on July 16, 2007
Accepted on July 16, 2007
Arabidopsis mutants lacking long chain base phosphate lyase are fumonisin sensitive and accumulate trihydroxy 18:1 long chain base phosphate
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