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In Vitro SUMOylation Assay to Study SUMO E3 Ligase Activity
Published on: January 29, 2018
Ubc9 acetylation modulates distinct SUMO target modification and hypoxia response
Yung-Lin Hsieh1, Hong-Yi Kuo, Che-Chang Chang
1Institute of Biomedical Sciences, Academia Sinica, Taipei, Taiwan, ROC.
The EMBO Journal
|February 12, 2013
Summary
Protein acetylation of Ubc9 selectively regulates sumoylation of specific substrates. This acetylation, influenced by hypoxia via SIRT1, impacts gene expression and cell survival, revealing a new regulatory pathway.
Area of Science:
- Biochemistry
- Molecular Biology
- Cellular Signaling
Background:
- Numerous substrates for small ubiquitin-like modifier (SUMO) conjugation are known, but regulatory mechanisms remain unclear.
- Differential regulation of substrate sumoylation is crucial for cellular processes.
Purpose of the Study:
- To investigate the regulatory mechanisms of substrate sumoylation.
- To identify signaling pathways that control Ubc9 activity and substrate sumoylation.
Main Methods:
- Investigated the effect of Ubc9 acetylation on sumoylation of various substrates.
- Analyzed Ubc9 binding to substrates with different SUMOylation motifs.
- Examined the role of hypoxia and SIRT1 in Ubc9 acetylation.
- Assessed the impact of Ubc9 acetylation on target gene expression and cell survival.
Main Results:
- Acetylation of Ubc9 at K65 selectively downregulates sumoylation of NDSM substrates (e.g., CBP, Elk-1).
- Ubc9 K65 acetylation reduces binding to NDSM substrates.
- Hypoxia downregulates Ubc9 K65 acetylation via SIRT1, affecting sumoylation and gene expression of CBP/Elk-1.
- Ubc9 acetylation modulates hypoxia response and cell survival.
Conclusions:
- Ubc9 acetylation/deacetylation acts as a dynamic switch for NDSM substrate sumoylation.
- A novel SIRT1/Ubc9 regulatory axis modulates protein sumoylation and hypoxia response.
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