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SUMOylation-regulated protein phosphorylation, evidence from quantitative phosphoproteomics analyses.

ABSTRACT: Protein modification is critical for the regulation of protein functions. Cross-talks among different types of protein modifications should yield concerted and coordinated regulatory networks for physiological functions. Here we have employed system-wide and quantitative phosphoproteomics analyses to reveal a global cross-talk for SUMOylation-modulated phosphorylation. Furthermore, as specific examples, we have shown that the ? subunit of casein kinase II is SUMOylated and that this affects the phosphorylation of its substrates. SUMO-regulated phosphorylation is involved in cell cycle control. Our data demonstrate an interplay between protein SUMOylation and phosphorylation and imply a regulatory role for this SUMOylation-modulated phosphorylation.

SUBMITTER: Yao Q 

PROVIDER: S-EPMC3149328 | biostudies-other | 2011 Aug

REPOSITORIES: biostudies-other

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SUMOylation-regulated protein phosphorylation, evidence from quantitative phosphoproteomics analyses.

Yao Qi Q   Li Hui H   Liu Bing-Qian BQ   Huang Xin-Yun XY   Guo Lin L  

The Journal of biological chemistry 20110617 31

Protein modification is critical for the regulation of protein functions. Cross-talks among different types of protein modifications should yield concerted and coordinated regulatory networks for physiological functions. Here we have employed system-wide and quantitative phosphoproteomics analyses to reveal a global cross-talk for SUMOylation-modulated phosphorylation. Furthermore, as specific examples, we have shown that the α subunit of casein kinase II is SUMOylated and that this affects the  ...[more]