The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility

@article{Pandithage2008TheRO,
  title={The regulation of SIRT2 function by cyclin-dependent kinases affects cell motility},
  author={Ruwin Pandithage and Richard Lilischkis and Kai Harting and Alexandra Wolf and Britta Jedamzik and Juliane M L{\"u}scher-Firzlaff and J{\"o}rg Vervoorts and Edwin Lasonder and Elisabeth Kremmer and Bernd Kn{\"o}ll and Bernhard L{\"u}scher},
  journal={The Journal of Cell Biology},
  year={2008},
  volume={180},
  pages={915 - 929}
}
Cyclin-dependent kinases (Cdks) fulfill key functions in many cellular processes, including cell cycle progression and cytoskeletal dynamics. A limited number of Cdk substrates have been identified with few demonstrated to be regulated by Cdk-dependent phosphorylation. We identify on protein expression arrays novel cyclin E-Cdk2 substrates, including SIRT2, a member of the Sirtuin family of NAD(+)-dependent deacetylases that targets alpha-tubulin. We define Ser-331 as the site phosphorylated by… CONTINUE READING
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