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Activation of sphingosine kinase 1 by ERK1/2‐mediated phosphorylation
It is shown that phosphorylation of sphingosine kinase 1 at Ser225 results not only in an increase in enzyme activity, but is also necessary for translocation of the enzyme from the cytosol to the plasma membrane.
Regulation of sphingosine kinase and sphingolipid signaling.
  • S. Pitson
  • Biology, Chemistry
    Trends in biochemical sciences
  • 1 February 2011
An oncogenic role of sphingosine kinase
Sphingosine kinase interacts with TRAF2 and dissects tumor necrosis factor-alpha signaling.
A role for SphK in the signal transduction by TRAF2 specifically leading to activation of NF-kappa B and antiapoptosis is shown, and it is shown that the interaction of TRAf2 with SphK and subsequent activation of SphK are critical for prevention of apoptosis during TNF stimulation.
Phosphorylation-dependent translocation of sphingosine kinase to the plasma membrane drives its oncogenic signalling
It is demonstrated, through constitutive localization of the phosphorylation-deficient form of h SK1 to the plasma membrane, that hSK1 translocation is the key effect ofosphorylation in oncogenic signaling by this enzyme.
Sphingosine Kinase Modulates Microvascular Tone and Myogenic Responses Through Activation of RhoA/Rho Kinase
It is reported that resting tone and myogenic responses of isolated resistance arteries increased with forced expression of Sphk1 in smooth muscle cells of these arteries, suggesting that Sphk 1 may play an important role in the control of peripheral resistance.
Translocation of Sphingosine Kinase 1 to the Plasma Membrane Is Mediated by Calcium- and Integrin-binding Protein 1*
This work demonstrates the requirement of CIB1-mediated translocation of SK1 in controlling cellular sphingosine 1-phosphate generation and associated anti-apoptotic signaling and functions as a Ca2+-myristoyl switch.
Expression of a Catalytically Inactive Sphingosine Kinase Mutant Blocks Agonist-induced Sphingosine Kinase Activation
The dominant-negative sphingosine kinase, hSKG82D, is employed to demonstrate that TNFα activation of extracellular signal-regulated kinases 1 and 2 (ERK1,2) is dependent on SK activation.