Sphingosine (Sph) is formed by the action of ceramidase (CDase) enzymes on ceramide in the lysosome.  Sph can also be formed in the extracellular (outer leaflet) side of the plasma membrane by the action of neutral CDase enzyme.  Sph then is either recycled back to ceramide or phosphorylated by one of the sphingosine kinase enzymes, SK1 and SK2. The product sphingosine-1-phosphate (S1P) can be dephosphorylated in the ER to regenerate sphingosine by certain S1P phosphatase enzymes within cells, where the salvaged Sph is recycled to ceramide.  Sphingosine is a single-chain lipid (usually 18 carbons in length), rendering it to have sufficient solubility in water. This explains its ability to move between membranes and to flip-flop across a membrane.  Estimates conducted at physiological pH show that approximately 70% of sphingosine remains in membranes while the remaining 30% is water-soluble. Sph that is formed has sufficient solubility in the liquid found inside cells (cytosol). Thus, Sph may come out of the lysosome and move to the ER without the need for transport via proteins or membrane-enclosed sacs called vesicles. However, its positive charge favors partitioning in lysosomes. It is proposed that the role of SK1 located near or in the lysosome is to ‘trap’ Sph via phosphorylation.
It is important to note that since sphingosine exerts surfactant activity, it is one of the sphingolipids found at lowest cellular levels.  The low levels of Sph and their increase in response to stimulation of cells, primarily by activation of ceramidase by growth-inducing proteins such as platelet-derived growth factor and insulin-like growth factor, is consistent with its function as a second messenger. It was found that immediate hydrolysis of only 3 to 10% of newly generated ceramide may double the levels of Sph. Treatment of HL60 cells (a type of leukemia cell line) by a plant-derived organic compound called phorbol ester increased Sph levels threefold, whereby the cells differentiated into white blood cells called macrophages.  Treatment of the same cells by exogenous Sph caused apoptosis. A specific protein kinase phosphorylates 14-3-3, otherwise known as sphingosine-dependent protein kinase 1 (SDK1), only in the presence of Sph.
Sph is also known to interact with protein targets such as the protein kinase H homologue (PKH) and the yeast protein kinase (YPK). These targets in turn mediate the effects of Sph and its related sphingoid bases, with known roles in regulating the actin cytoskeleton, endocytosis, the cell cycle and apoptosis.  It is important to note however that the second messenger function of Sph is not yet established unambiguously.