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Dual Site Mechanism Governs Sphingosine Kinase 1 Membrane Binding and Biological Function

Sphingosine kinase 1 (SK1) is an enzyme at a critical junction in sphingolipid metabolism as it can regulate the balance between the pro‐apoptotic lipids ceramide and sphingosine and the pro‐survival lipid sphingosine 1‐phosphate. Here we identify a novel membrane binding motif in SK1 which is responsible for interaction with anionic phospholipids in the membrane, such as phosphatidic acid (PA). We believe that this newly identified site works in conjunction with a previously identified hydrophobic site in order to regulate the biological function of SK1. In vitro biochemical analysis shows that the anionic binding site is responsible for binding to PA. However, both sites are needed to effectively bind to liposomes containing PA. This provides evidence for SK1's binding to membranes being dictated by both sites. In cells, these sites are important for membrane binding as shown in both fractionation experiments as well as membrane localization by confocal imaging. However, this effect isn't limited to biochemical observations as these sites also affect the biology of SK1.