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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
Published on: January 29, 2018
Sumoylation of CoREST modulates its function as a transcriptional repressor
Ayako Muraoka1, Atsuyo Maeda, Norie Nakahara
1Faculty of Pharmaceutical Sciences at Kagawa Campus, Tokushima Bunri University, 1314-1 Shido, Sanuki, Kagawa 769-2193, Japan.
Biochemical and Biophysical Research Communications
|October 16, 2008
Summary
Small ubiquitin-like modifier (SUMO) modification regulates gene transcription. SUMO-1 modification of Co-Repressor for Element 1 (CoREST) at lysine 294 enhances its repressive activity, crucial for full corepressor function.
Area of Science:
- Molecular Biology
- Epigenetics
- Gene Regulation
Background:
- Covalent modifications, particularly SUMOylation, play a critical role in regulating transcription factors and co-factors.
- SUMOylation is frequently linked to transcriptional repression, suggesting its involvement in corepressor activity.
Purpose of the Study:
- To investigate the role of SUMOylation in modulating the repressive activity of Co-Repressor for Element 1 (CoREST).
- To identify the specific SUMO modification site on CoREST and the enzymes involved in its regulation.
Main Methods:
- In vitro and in vivo interaction studies to identify CoREST-interacting proteins.
- SUMOylation and desumoylation assays using recombinant proteins and cell lysates.
- Site-directed mutagenesis to investigate the functional significance of the SUMOylation site on CoREST.
Main Results:
- CoREST was identified as being modified by SUMO-1 at lysine 294.
- PIASxbeta was found to interact with CoREST and function as an E3-ligase for its sumoylation.
- SENP1 mediated the desumoylation of CoREST, and mutation of the SUMOylation site impaired CoREST's corepressor function.
Conclusions:
- SUMO-1 modification at lysine 294 is a key regulatory mechanism for CoREST's transcriptional repressive activity.
- The sumoylation and desumoylation of CoREST, mediated by PIASxbeta and SENP1 respectively, are essential for its full corepressor function.
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