Megidish T, White T, Takio K, Titani K, Igarashi Y, Hakomori S
Biomembrane Institute, Seattle, WA 98119, USA.
Biochem Biophys Res Commun. 1995 Nov 22;216(3):739-47. doi: 10.1006/bbrc.1995.2684.
Phosphorylation of a 28 kDa protein in 3T3(A31) cells upon addition of semi-purified kinase was induced only by sphingosine (Sph) or N,N-dimethylsphingosine (DMS), but not by 17 other lipids tested. The 28 kDa protein, a major target of Sph- or DMS-dependent kinase, is now identified as 14-3-3 protein, which modulates a number of key protein kinases involved in regulation of intracellular signaling (Aitken A, Trends Biochem Sci 20:95-97, 1995; Morrison D, Science 266:56-57, 1994). Thus, Sph and DMS modulate the function of a versatile modulator controlling a number of signaling molecules.