Phosphorylation Regulates SIRT1 Function
Author Information
Author(s): Sasaki Tsutomu, Maier Bernhard, Koclega Katarzyna D., Chruszcz Maksymilian, Gluba Wendy, Stukenberg P. Todd, Minor Wladek, Scrable Heidi
Primary Institution: University of Virginia
Hypothesis
Does phosphorylation regulate the deacetylase activity of SIRT1?
Conclusion
Phosphorylation by cell cycle-dependent kinases is a major mechanism controlling the level and function of SIRT1.
Supporting Evidence
- SIRT1 is phosphorylated at 13 residues in vivo.
- Dephosphorylation by phosphatases decreased SIRT1's deacetylase activity.
- CyclinB/Cdk1 phosphorylates SIRT1, affecting cell cycle progression.
- Phosphorylation of SIRT1 is necessary for normal cell cycle progression.
Takeaway
This study shows that a protein called SIRT1, which helps control cell growth, is regulated by being chemically modified through phosphorylation, especially during the cell cycle.
Methodology
Mass spectrometry was used to identify phosphorylated residues in SIRT1, and deacetylase activity was measured using fluorogenic peptide substrates.
Limitations
The study does not explore all potential phosphorylation sites or their effects on SIRT1's function in detail.
Statistical Information
P-Value
p<0.005
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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