Stimulation of nuclear sphingosine kinase activity by platelet-derived growth factor

FEBS Lett. 2001 Aug 10;503(1):85-90. doi: 10.1016/s0014-5793(01)02697-7.


Subcellular fractionation revealed that a significant fraction of total sphingosine kinase, the enzyme that phosphorylates sphingosine to form the bioactive lipid metabolite sphingosine-1-phosphate, resides in the nuclei of Swiss 3T3 cells, localized to both the nuclear envelope and the nucleoplasm. Platelet-derived growth factor, in addition to rapidly stimulating cytosolic sphingosine kinase, also induced a large increase in nucleoplasm-associated activity after 12-24 h that correlated with progression of cells to the S-phase of the cell cycle and translocation of sphingosine kinase-green fluorescent protein fusion protein to the nuclear envelope. Our results add sphingosine kinase to the growing list of lipid-metabolizing enzymes associated with the nucleus, and suggest that sphingosine-1-phosphate may also play a role in signal transduction in the nucleus.

Publication types

  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • 3T3 Cells
  • Animals
  • Cell Nucleus / enzymology*
  • Enzyme Activation
  • Green Fluorescent Proteins
  • Luminescent Proteins / genetics
  • Mice
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism*
  • Platelet-Derived Growth Factor / pharmacology*
  • Protein Transport
  • S Phase


  • Luminescent Proteins
  • Platelet-Derived Growth Factor
  • Green Fluorescent Proteins
  • Phosphotransferases (Alcohol Group Acceptor)
  • sphingosine kinase