SUMOylation-regulated protein phosphorylation, evidence from quantitative phosphoproteomics analyses.
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ABSTRACT:
SUBMITTER: Yao Q
PROVIDER: S-EPMC3149328 | biostudies-other | 2011 Aug
REPOSITORIES: biostudies-other
Publications
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]
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