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J Biol Chem. 2011 Aug 5;286(31):27342-9. doi: 10.1074/jbc.M111.220848. Epub 2011 Jun 17.

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

Author information

1
State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072 China.

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 α 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.

PMID:
21685386
PMCID:
PMC3149328
DOI:
10.1074/jbc.M111.220848
[Indexed for MEDLINE]
Free PMC Article

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