Regulation of histone acetylation in the nucleus by sphingosine-1-phosphate.
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ABSTRACT:
SUBMITTER: Hait NC
PROVIDER: S-EPMC2850596 | biostudies-literature | 2009 Sep
REPOSITORIES: biostudies-literature
Publications
Regulation of histone acetylation in the nucleus by sphingosine-1-phosphate.
Hait Nitai C NC Allegood Jeremy J Maceyka Michael M Strub Graham M GM Harikumar Kuzhuvelil B KB Singh Sandeep K SK Luo Cheng C Marmorstein Ronen R Kordula Tomasz T Milstien Sheldon S Spiegel Sarah S
Science (New York, N.Y.) 20090901 5945
The pleiotropic lipid mediator sphingosine-1-phosphate (S1P) can act intracellularly independently of its cell surface receptors through unknown mechanisms. Sphingosine kinase 2 (SphK2), one of the isoenzymes that generates S1P, was associated with histone H3 and produced S1P that regulated histone acetylation. S1P specifically bound to the histone deacetylases HDAC1 and HDAC2 and inhibited their enzymatic activity, preventing the removal of acetyl groups from lysine residues within histone tail ...[more]
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