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J. Biol. Chem., Vol. 279, Issue 43, 44763-44774, October 22, 2004
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¶
From the
Department of Signalling, Babraham Institute, Cambridge CB2 4AT and the Department of Physiology and Pharmacology, Strathclyde Institute for Biomedical Sciences, University of Strathclyde, Glasgow G4 0NR, United Kingdom
Sphingosine kinase 1 (SK1) phosphorylates sphingosine to generate sphingosine 1-phosphate (S1P). Because both substrate and product of the enzyme are potentially important signaling molecules, the regulation of SK1 is of considerable interest. We report that SK1, which is ordinarily a cytosolic enzyme, translocates in vivo and in vitro to membrane compartments enriched in phosphatidic acid (PA), the lipid product of phospholipase D. This translocation depends on direct interaction of SK1 with PA, because recombinant purified enzyme shows strong affinity for pure PA coupled to Affi-Gel. The SK1-PA interaction maps to the C terminus of SK1 and is independent of catalytic activity or of the diacylglycerol kinase-like domain of the enzyme. Thus SK1 constitutes a novel, physiologically relevant PA effector.
Received for publication, May 24, 2004 , and in revised form, July 30, 2004.
* This work was supported by the Biotechnology and Biological Sciences and Research Council (to C. D., M. M., E. W., and N. T. K.), the Medical Research Council (to D. T. and S. P.), and Cancer Research UK (to S. K.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
¶ To whom correspondence should be addressed. Tel.: 44-1223-496-323; Fax: 44-1223-496-043; E-mail: nicholas.ktistakis{at}bbsrc.ac.uk.
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