中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
Chemical Proteomic Profiling of Lysine Benzoylation

文献类型:期刊论文

作者Song, Xiaohan3; Lu, Yuhan2; Peng, Panpan1; Chen, Binjing3; Huang, He1,2,3,4
刊名JOURNAL OF PROTEOME RESEARCH
出版日期2026-02-04
页码9
关键词lysine benzoylation substrates chemical proteomic nucleophosmin
ISSN号1535-3893
DOI10.1021/acs.jproteome.5c00792
通讯作者Huang, He(hhuang@simm.ac.cn)
英文摘要Benzoylation (Kbz) is a physiologically relevant post-translational modification derived from the food additive sodium benzoate. While Kbz has been implicated in unique cellular regulatory processes, its substrate landscape and functional consequences remain poorly characterized. Conventional antibody-based enrichment methods for Kbz detection suffer from affinity bias and limited specificity. Here, we developed AyBz3, a bioorthogonal chemical probe enabling the unbiased mapping of Kbz across the proteome. Implementation of AyBz3 in HepG2 cells revealed 688 unique Kbz sites, significantly expanding the known benzoylome. Functional analysis revealed that Kbz-modified proteins are enriched in pathways related to protein translation and cell adhesion. Notably, we demonstrated that Kbz modification of nucleophosmin 1 (NPM1) impairs its molecular chaperone function toward p53, resulting in accelerated p53 degradation. Together, this study establishes AyBz3 as a powerful probe for unbiased benzoylome profiling and provides new insights into the regulatory roles of Kbz in cellular processes.
WOS关键词METABOLIC-REGULATION ; GENE-EXPRESSION ; NUCLEOPHOSMIN ; REPORTERS
资助项目Chinese Academy of Sciences[XDB1060000] ; Taishan Scholar Project of Shandong Province[tstp20240845] ; Science and Technology Commission of Shanghai Municipality[NA] ; Department of Science and Technology of Shandong Province[SYS202205] ; Hangzhou Institute for Advanced Study, University of Chinese Academy of Sciences[NA] ; Hangzhou Municipal Government[NA] ; Natural Science Foundation of Shanghai Municipality[23ZR1474600] ; Natural Science Foundation of Shandong Province[ZR2024MB112] ; Key Technology Research and Development Program of Shandong Province[2024CXPT028] ; National Natural Science Foundation of China[22277125]
WOS研究方向Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:001683972500001
出版者AMER CHEMICAL SOC
源URL[http://119.78.100.183/handle/2S10ELR8/322842]  
专题中国科学院上海药物研究所
通讯作者Huang, He
作者单位1.Chinese Acad Sci, Shanghai Inst Mat Med, State Key Lab Chem Biol, Shanghai 201203, Peoples R China
2.Nanjing Univ Chinese Med, Sch Chinese Mat Med, Nanjing 210023, Peoples R China
3.Univ Chinese Acad Sci, Hangzhou Inst Adv Study, Sch Pharmaceut Sci & Technol, Key Lab Glyco Drug Res Zhejiang Prov, Hangzhou 310024, Peoples R China
4.Bohai Rim Adv Res Inst Drug Discovery, Shandong Lab Yantai Drug Discovery, Yantai 264117, Peoples R China
推荐引用方式
GB/T 7714
Song, Xiaohan,Lu, Yuhan,Peng, Panpan,et al. Chemical Proteomic Profiling of Lysine Benzoylation[J]. JOURNAL OF PROTEOME RESEARCH,2026:9.
APA Song, Xiaohan,Lu, Yuhan,Peng, Panpan,Chen, Binjing,&Huang, He.(2026).Chemical Proteomic Profiling of Lysine Benzoylation.JOURNAL OF PROTEOME RESEARCH,9.
MLA Song, Xiaohan,et al."Chemical Proteomic Profiling of Lysine Benzoylation".JOURNAL OF PROTEOME RESEARCH (2026):9.

入库方式: OAI收割

来源:上海药物研究所

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