title: 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 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.
authors.affiliation: State Key Laboratory of Virology, College of Life Sciences, Wuhan University, Wuhan 430072 China.
authors.forename: Qi
authors.initials: Q
authors.lastname: Yao
authors.forename: Hui
authors.initials: H
authors.lastname: Li
authors.forename: Bing-Qian
authors.initials: BQ
authors.lastname: Liu
authors.forename: Xin-Yun
authors.initials: XY
authors.lastname: Huang
authors.forename: Lin
authors.initials: L
authors.lastname: Guo
mesh_terms: D001483:Base Sequence; D002453:Cell Cycle / Q000502:physiology; D002460:Cell Line; D002850:Chromatography, Gel; D017931:DNA Primers; D006801:Humans; D010750:Phosphoproteins / Q000378:metabolism*; D010766:Phosphorylation; D040901:Proteomics; D025842:SUMO-1 Protein / Q000502:physiology*; D058207:Sumoylation; D053719:Tandem Mass Spectrometry
chemical_list: D017931:DNA Primers; D010750:Phosphoproteins; D025842:SUMO-1 Protein