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Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
Published on: February 27, 2016
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Src regulates the activity of SIRT2
You Hee Choi1, Hangun Kim2, Sung Ho Lee1
1College of Pharmacy and Research Institute of Drug Development, Chonnam National University, Gwangju, South Korea.
Biochemical and Biophysical Research Communications
|July 5, 2014
Summary
The tyrosine kinase Src reduces levels of SIRT2 (Sirtuin 2) by phosphorylating it. This interaction impacts SIRT2
Area of Science:
- Biochemistry
- Cell Biology
- Molecular Signaling
Background:
- SIRT2 is a key NAD(+)-dependent deacetylase in mammals.
- The tyrosine kinase Src regulates crucial cellular processes like proliferation and DNA synthesis.
- The interaction and regulatory mechanism between SIRT2 and c-Src remain unclear.
Purpose of the Study:
- To investigate the regulation of SIRT2 function by c-Src.
- To elucidate the molecular signaling pathway involving c-Src and SIRT2.
Main Methods:
- Utilized c-Src to modulate SIRT2 protein levels.
- Employed a Src-specific inhibitor (SU6656) and siRNA for c-Src knockdown.
- Investigated c-Src interaction and phosphorylation of SIRT2 at Tyr104.
- Assessed the impact of c-Src on SIRT2 deacetylation activity.
Main Results:
- c-Src significantly decreased SIRT2 protein levels.
- Src inhibition or knockdown restored SIRT2 protein levels.
- c-Src directly interacts with and phosphorylates SIRT2 at Tyr104.
- Phosphorylation of SIRT2 by c-Src influences its deacetylation activity.
Conclusions:
- c-Src negatively regulates SIRT2 protein levels and function.
- Phosphorylation at Tyr104 is a key mechanism for c-Src-mediated SIRT2 regulation.
- This study reveals a novel signaling pathway involving c-Src and SIRT2.
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