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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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SIRT2 regulates nuclear envelope reassembly through ANKLE2 deacetylation
Tanja Kaufmann1,2, Eva Kukolj1, Andreas Brachner1
1Department of Biochemistry, Max F. Perutz Laboratories, University of Vienna, Dr Bohr-Gasse 9, Vienna 1030, Austria.
Journal of Cell Science
|November 23, 2016
Summary
Sirtuin 2 (SIRT2) depletion or overexpression disrupts nuclear envelope reassembly. This is linked to ANKLE2 regulation, revealing SIRT2
Area of Science:
- Molecular and Cell Biology
- Epigenetics and Post-Translational Modifications
Background:
- Sirtuin 2 (SIRT2) is an NAD-dependent deacetylase.
- SIRT2 is known to regulate microtubule dynamics and cell cycle progression.
- SIRT2 is implicated in cancer, neurodegenerative diseases, and progeria.
Purpose of the Study:
- To investigate the role of SIRT2 in nuclear envelope reassembly.
- To identify novel functions of SIRT2 beyond microtubule regulation.
Main Methods:
- SIRT2 depletion and overexpression experiments.
- Analysis of nuclear envelope reassembly dynamics.
- Investigation of ANKLE2 acetylation and phosphorylation.
Main Results:
- SIRT2 depletion or overexpression causes nuclear envelope reassembly defects.
- ANKLE2 acetylation at K302 and phosphorylation at S662 are regulated by SIRT2.
- SIRT2-mediated regulation of ANKLE2 is essential for nuclear envelope reassembly.
Conclusions:
- SIRT2 plays a critical role in nuclear envelope dynamics.
- The function of SIRT2 extends to the regulation of nuclear envelope reassembly through ANKLE2.
- This finding broadens the understanding of SIRT2's cellular functions and potential therapeutic implications.
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