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Characterization of endogenous SUMOylation sites by click chemistry-based proteomics

文献类型：期刊论文

作者Ma, Ke5; Chen, Sixian4; Zhang, Jun2,3; Jia, Xinglong3; Fan, Rufeng2,3; Li, Mingjun5; Dong, Li1; Tan, Minjia1,2,3,4; Zhao, Wensi5; Xie, Dong5
刊名ANALYTICAL AND BIOANALYTICAL CHEMISTRY
出版日期2025-06-16
页码15
关键词SUMOylation Click chemistry Proteomics Post-translational modification
ISSN号1618-2642
DOI10.1007/s00216-025-05957-2
英文摘要SUMOylation, an essential ubiquitin-like modification in eukaryotes, plays vital roles in both physiological and pathological regulation, positioning it as a promising therapeutic target. However, the low abundance of SUMOylation and the high enzymatic activity of sentrin/SUMO-specific proteases (SENPs) complicate the identification of endogenous sites. In this study, we integrated click chemistry, acid cleavage, and SUMOylated peptide enrichment into the workflow and developed a promising methodology for system-wide identification of SUMOylation sites. In total, we identified 962 endogenous SUMOylation sites in HEK293T cells under heat shock conditions, which showed good complementarity with previous studies. Our approach uncovered 105 potentially new sites, including SSRP1-K248/K319/K612, DHX9-K806, and ILF3-K241, which showed high conservation and were located in functionally important domains. The overlap between SUMOylation sites and the known ubiquitination or acetylation sites suggested the potential PTM crosstalks. KEGG analysis further suggested SUMOylated proteins were associated with carbon metabolism and biosynthesis of amino acids pathways. Collectively, this study provides a valuable tool for systematically identifying SUMOylation sites, advancing further biological understanding of their dynamic regulatory networks and pathophysiological mechanisms.
WOS关键词POSTTRANSLATIONAL MODIFICATIONS ; DHX9 HELICASE ; SUMO ; REVEALS ; IDENTIFICATION ; OPTIMIZATION ; ACETYLATION ; TARGETS ; DOMAIN ; CELLS
资助项目National Natural Science Foundation of China[82272943] ; Science and Technology Commission of Shanghai Municipality[21Y11913400]
WOS研究方向Biochemistry & Molecular Biology ; Chemistry
语种英语
WOS记录号WOS:001509394000001
出版者SPRINGER HEIDELBERG
源URL[http://119.78.100.183/handle/2S10ELR8/318380]  
专题新药研究国家重点实验室
通讯作者Zhao, Wensi; Xie, Dong
作者单位1.Chinese Acad Sci, Zhongshan Inst Drug Discovery, Shanghai Inst Mat Med, Zhongshan 528400, Peoples R China
2.Univ Chinese Acad Sci, Beijing 101408, Peoples R China
3.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Drug Res, Shanghai 201203, Peoples R China
4.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Jiangsu, Peoples R China
5.Tongji Univ, Shanghai Pulm Hosp, Sch Med, Dept Thorac Surg, Shanghai 200433, Peoples R China
推荐引用方式
GB/T 7714		 Ma, Ke,Chen, Sixian,Zhang, Jun,et al. Characterization of endogenous SUMOylation sites by click chemistry-based proteomics[J]. ANALYTICAL AND BIOANALYTICAL CHEMISTRY,2025:15.
APA Ma, Ke.,Chen, Sixian.,Zhang, Jun.,Jia, Xinglong.,Fan, Rufeng.,...&Xie, Dong.(2025).Characterization of endogenous SUMOylation sites by click chemistry-based proteomics.ANALYTICAL AND BIOANALYTICAL CHEMISTRY,15.
MLA Ma, Ke,et al."Characterization of endogenous SUMOylation sites by click chemistry-based proteomics".ANALYTICAL AND BIOANALYTICAL CHEMISTRY (2025):15.

入库方式： OAI收割

来源：上海药物研究所

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