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Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates
14:32

Deacetylation Assays to Unravel the Interplay between Sirtuins SIRT2 and Specific Protein-substrates

Published on: February 27, 2016

7.8K

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
PubMed

Insights

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.
Keywords:
PhosphorylationProtein levelSIRT2Src

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