DICP OpenIR
Combinatorial Peptide Ligand Library-Based Photoaffinity Probe for the Identification of Phosphotyrosine-Binding Domain Proteins
An, Jinying1; Zhai, Guijin1; Guo, Zhenchang1; Bai, Xue1; Chen, Pu1; Dong, Hanyang1; Tian, Shanshan1; Ai, Ding2; Zhang, Yukui3; Zhang, Kai1
Corresponding AuthorZhai, Guijin(zhaiguijin@tmu.edu.cn) ; Zhang, Kai(kzhang@tmu.edu.cn)
Source PublicationANALYTICAL CHEMISTRY
2019-03-05
ISSN0003-2700
DOI10.1021/acs.analchem.8b04781
Volume91Issue:5Pages:3221-3226
Funding ProjectNational Natural Science Foundation of China[21874100] ; National Natural Science Foundation of China[21275077] ; National Natural Science Foundation of China[21705067] ; National Basic Research Program of China[2016YFC0903000] ; Tianjin Medical University
Funding OrganizationNational Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University
WOS SubjectChemistry, Analytical
WOS Research AreaChemistry
WOS KeywordTYROSINE PHOSPHORYLATION ; SH2 DOMAIN ; SPECIFICITY ; PROTEOME ; TARGET ; SITES
AbstractPhosphotyrosine (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.
Language英语
Funding OrganizationNational Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University ; National Natural Science Foundation of China ; National Natural Science Foundation of China ; National Basic Research Program of China ; National Basic Research Program of China ; Tianjin Medical University ; Tianjin Medical University
WOS IDWOS:000460709200009
PublisherAMER CHEMICAL SOC
Citation statistics
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/165903
Collection中国科学院大连化学物理研究所
Corresponding AuthorZhai, Guijin; Zhang, Kai
Affiliation1.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
Recommended Citation
GB/T 7714
An, Jinying,Zhai, Guijin,Guo, Zhenchang,et al. Combinatorial Peptide Ligand Library-Based Photoaffinity Probe for the Identification of Phosphotyrosine-Binding Domain Proteins[J]. ANALYTICAL CHEMISTRY,2019,91(5):3221-3226.
APA An, Jinying.,Zhai, Guijin.,Guo, Zhenchang.,Bai, Xue.,Chen, Pu.,...&Zhang, Kai.(2019).Combinatorial Peptide Ligand Library-Based Photoaffinity Probe for the Identification of Phosphotyrosine-Binding Domain Proteins.ANALYTICAL CHEMISTRY,91(5),3221-3226.
MLA An, Jinying,et al."Combinatorial Peptide Ligand Library-Based Photoaffinity Probe for the Identification of Phosphotyrosine-Binding Domain Proteins".ANALYTICAL CHEMISTRY 91.5(2019):3221-3226.
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