Functional analyses of differentially expressed isoforms of the Arabidopsis inositol phosphorylceramide synthase

Sphingolipids are key components of eukaryotic plasma membranes that are involved in many functions, including the formation signal transduction complexes. In addition, these lipid species and their catabolites function as secondary signalling molecules in, amongst other processes, apoptosis. The bi...

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Published inPlant molecular biology Vol. 73; no. 4-5; pp. 399 - 407
Main Authors Mina, J. G, Okada, Y, Wansadhipathi-Kannangara, N. K, Pratt, S, Shams-Eldin, H, Schwarz, R. T, Steel, P. G, Fawcett, T, Denny, P. W
Format Journal Article
LanguageEnglish
Published Dordrecht Dordrecht : Springer Netherlands 01.07.2010
Springer Netherlands
Springer Nature B.V
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Summary:Sphingolipids are key components of eukaryotic plasma membranes that are involved in many functions, including the formation signal transduction complexes. In addition, these lipid species and their catabolites function as secondary signalling molecules in, amongst other processes, apoptosis. The biosynthetic pathway for the formation of sphingolipid is largely conserved. However, unlike mammalian cells, fungi, protozoa and plants synthesize inositol phosphorylceramide (IPC) as their primary phosphosphingolipid. This key step involves the transfer of the phosphorylinositol group from phosphatidylinositol (PI) to phytoceramide, a process catalysed by IPC synthase in plants and fungi. This enzyme activity is at least partly encoded by the AUR1 gene in the fungi, and recently the distantly related functional orthologue of this gene has been identified in the model plant Arabidopsis. Here we functionally analysed all three predicted Arabidopsis IPC synthases, confirming them as aureobasidin A resistant AUR1p orthologues. Expression profiling revealed that the genes encoding these orthologues are differentially expressed in various tissue types isolated from Arabidopsis.
Bibliography:http://dx.doi.org/10.1007/s11103-010-9626-3
ISSN:0167-4412
1573-5028
DOI:10.1007/s11103-010-9626-3