Picture of scraped petri dish

Scrape below the surface of Strathprints...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs. Explore world class Open Access research by researchers at Strathclyde, a leading technological university.

Explore

Sphingosine kinase 1 is an intracellular effector of phosphatidic acid

Delon, C. and Manifava, M. and Wood, E. and Thompson, D. and Krugmann, S. and Pyne, S. and Ktistakis, N.T. (2004) Sphingosine kinase 1 is an intracellular effector of phosphatidic acid. Journal of Biological Chemistry, 279. pp. 44763-44774. ISSN 0021-9258

Full text not available in this repository. (Request a copy from the Strathclyde author)

Abstract

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.