Combinatorial Peptide Ligand Library-Based Photoaffinity Probe for the Identification of Phosphotyrosine-Binding Domain Proteins

被引:4
|
作者
An, Jinying [1 ]
Zhai, Guijin [1 ]
Guo, Zhenchang [1 ]
Bai, Xue [1 ]
Chen, Pu [1 ]
Dong, Hanyang [1 ]
Tian, Shanshan [1 ]
Ai, Ding [2 ]
Zhang, Yukui [3 ]
Zhang, Kai [1 ]
机构
[1] Tianjin Med Univ, Canc Inst & Hosp,Collaborat Innovat Ctr Tianjin M, Tianjin Key Lab Med Epigenet,Key Lab Breast Canc, Key Lab Immune Microenvironm & Dis,Minist Educ,De, Tianjin 300070, Peoples R China
[2] Tianjin Med Univ, Dept Physiol & Pathophysiol, Tianjin Key Lab Metab Dis, Tianjin 300070, Peoples R China
[3] Chinese Acad Sci, Dalian Inst Chem Phys, 457 Zhongshan Rd, Dalian 116023, Peoples R China
基金
中国国家自然科学基金;
关键词
TYROSINE PHOSPHORYLATION; SH2; DOMAIN; SPECIFICITY; PROTEOME; TARGET; SITES;
D O I
10.1021/acs.analchem.8b04781
中图分类号
O65 [分析化学];
学科分类号
070302 ; 081704 ;
摘要
Phosphotyrosine (pY) serves as a docking site for the recognition proteins containing pY-binding (pYB) modules, such as the SH2 domain, to mediate cell signal transduction. Thus, it is vital to profile these binding proteins for understanding of signal regulation. However, identification of pYB proteins remains a significant challenge due to their low abundance and typically weak and transient interactions with pY sites. Herein, we designed and prepared a pY-peptide photoaffinity probe for the robust and specific enrichment and identification of its binding proteins. Using SHC1-pY(317) as a paradigm, we showed that the developed probe enables to capture target protein with high selectivity and remarkable specificity even in a complex context. Notably, we expanded the strategy to a combinatorial pY-peptide-based photoaffinity probe by using combinatorial peptide ligand library (CPLL) technique and identified 24 SH2 domain proteins, which presents a deeper profiling of pYB proteins than previous reports using affinity probes. Moreover, the method can be used to mine putative pYB proteins and confirmed PKN2 as a selective binder to pY, expanding the repertoire of known domain proteins. Our approach provides a general strategy for rapid and robust interrogating pYB proteins and will promote the understanding of the signal transduction mechanism.
引用
收藏
页码:3221 / 3226
页数:6
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