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Entry URI http://metadb.riken.jp/db/SciNetS_ria224i/cria224u4ria224u17635905i
Entry name Tsegaye Yoseph et al. 2007 Sep. J. Biol. Chem. 282(38):28195-206.
Title Arabidopsis mutants lacking long chain base phosphate lyase are fumonisin-sensitive and accumulate trihydroxy-18:1 long chain base phosphate.
Authors Bravo Janis E|Cahoon Edgar B|Chen Ming|Dunn Teresa M|Jaworski Jan G|Lynch Daniel V|Markham Jonathan E|Mulcahy Brendan J|Richardson Christopher G|Tsegaye Yoseph
Abstract The sphingoid long chain bases (LCBs) and their phosphorylated derivatives (LCB-Ps) are important signaling molecules in eukaryotic organisms. The cellular levels of LCB-Ps are tightly controlled by the coordinated action of the LCB kinase activity responsible for their synthesis and the LCB-P phosphatase and lyase activities responsible for their catabolism. Although recent studies have implicated LCB-Ps as regulatory molecules in plants, in comparison with 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 remarkably 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 B(1).
Pubmed ID 17635905
Journal The Journal of biological chemistry
Volume 282
Issue 38
Pages 28195-206
Publication date 2007 Sep
Num of phenotype gene 0