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Updated: May 31, 2026
15:41
Quantitative Phosphoproteomics in Fatty Acid Stimulated Saccharomyces cerevisiae
Published on: October 12, 2009
SUMOylation-regulated protein phosphorylation, evidence from quantitative phosphoproteomics analyses
Qi Yao1, Hui Li, Bing-Qian Liu
1State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072 China.
The Journal of Biological Chemistry
|June 21, 2011
Summary
This study reveals a global cross-talk between SUMOylation and phosphorylation, demonstrating how SUMOylation regulates protein phosphorylation. This interplay is crucial for physiological functions, including cell cycle control.
Area of Science:
- Biochemistry
- Molecular Biology
- Cell Biology
Background:
- Protein modifications like SUMOylation and phosphorylation are essential for regulating protein function.
- Coordinated regulation through cross-talk between different modifications is vital for cellular processes.
Purpose of the Study:
- To investigate the global cross-talk between SUMOylation and phosphorylation.
- To elucidate the regulatory role of SUMOylation in modulating phosphorylation events.
- To explore the involvement of SUMOylation-modulated phosphorylation in cell cycle control.
Main Methods:
- System-wide and quantitative phosphoproteomics analyses were employed.
- Specific protein interactions and modifications were examined.
- Functional relevance in cell cycle control was assessed.
Main Results:
- A global cross-talk between SUMOylation and phosphorylation was identified.
- The alpha subunit of casein kinase II was found to be SUMOylated, impacting its substrate phosphorylation.
- SUMOylation-regulated phosphorylation plays a role in cell cycle regulation.
Conclusions:
- Protein SUMOylation and phosphorylation exhibit a significant interplay.
- SUMOylation-modulated phosphorylation is implied to have a regulatory role in cellular functions.
- This cross-talk provides insights into coordinated regulatory networks in physiology.
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