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J Biol Chem, Vol. 273, Issue 31, 19437-19442, July 31, 1998
From the Department of Biochemistry and the Lucille P. Markey
Cancer Center, University of Kentucky Medical Center,
Lexington, Kentucky 40536-0084
Sphingolipid long chain bases (LCBs) and
phosphorylated derivatives, particularly sphingosine 1-phosphate, are
putative signaling molecules. To help elucidate the physiological roles
of LCB phosphates, we identified two Saccharomyces
cerevisiae genes, LCB4 (YOR171c) and
LCB5 (YLR260w), which encode LCB kinase
activity. This conclusion is based upon the synthesis of LCB kinase
activity in Escherichia coli expressing either
LCB gene. LCB4 encodes most (97%)
Saccharomyces LCB kinase activity, with the remainder
requiring LCB5. Log phase lcb4-deleted yeast
cells make no LCB phosphates, showing that the Lcb4 kinase synthesizes
all detectable LCB phosphates under these growth conditions. The Lcb4
and Lcb5 proteins are paralogs with 53% amino acid identity but are
not related to any known protein, thus revealing a new class of lipid
kinase. Two-thirds of the Lcb4 and one-third of the Lcb5 kinase
activity are in the membrane fraction of yeast cells, a puzzling
finding in that neither protein contains a membrane-localization
signal. Both enzymes can use phytosphingosine, dihydrosphingosine, or
sphingosine as substrate. LCB4 and LCB5 should
be useful for probing the functions of LCB phosphates in S. cerevisiae. Potential mammalian cDNA homologs of the LCB
kinase genes may prove useful in helping to understand the function of
sphingosine 1-phosphate in mammals.
The LCB4 (YOR171c) and LCB5
(YLR260w) Genes of Saccharomyces Encode
Sphingoid Long Chain Base Kinases
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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