Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells
Li, Siting1,3; Chen, Minghai2,3; Xiong, Qian1; Zhang, Jia1; Cui, Zongqiang2; Ge, Feng1
2016-10-01
Source PublicationJOURNAL OF PROTEOME RESEARCH
ISSN1535-3893
Volume15Issue:10Pages:3741-3751
AbstractTranslationally controlled tumor protein (TCTP) is a highly conserved housekeeping protein present in eukaryotic organisms. It is involved in regulating many fundamental processes and plays a critical role in tumor reversion and tumorigenesis. Increasing evidence suggests that TCTP plays a role in the regulation of cell fate determination and is a promising therapeutic target for cancer. To decipher the exact mechanisms by which TCTP functions and how all these functions are integrated, we analyzed the interactome of TCTP in HeLa cells by coimmunoprecipitation (IP) and mass spectrometry (MS). A total of 98 proteins were identified. We confirmed the in vitro and in vivo association of TCTP with six of the identified binding proteins using reciprocal IP and bimolecular fluorescence complementation (BiFC) analysis, respectively. Moreover, TCTP interacted with Y-box-binding protein 1 (YBX1), and their interaction was localized to the N-terminal region of TCTP and the 1-129 amino acid (aa) residues of YBX1. The YBX1 protein plays an important role in cell proliferation, RNA splicing, DNA repair, drug resistance, and stress response to extracellular signals. These data suggest that the interaction of TCTP with YBX1 might cooperate or coordinate their functions in the control of diverse regulatory pathways in cancer cells. Taken together, our results not only reveal a large number of TCTP-associated proteins that possess pleiotropic functions, but also provide novel insights into the molecular mechanisms of TCTP in tumorigenesis.
SubtypeArticle
KeywordTranslationally Controlled Tumor Protein (Tctp) Mass Spectrometry (Ms) Coimmunoprecipitation (Co-ip) Bimolecular Fluorescence Complementation (Bifc) Peroxiredoxin 1 (Prdx1) Y-box-binding Protein 1 (Ybx1)
DOI10.1021/acs.jproteome.6b00556
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
Indexed BySCI
Funding OrganizationNational Key Research and Development Program(2016YFA0501304) ; National Key Research and Development Program(2016YFA0501304) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; National Natural Science Foundation of China(31570829) ; National Natural Science Foundation of China(31570829) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202) ; National Key Research and Development Program(2016YFA0501304) ; National Key Research and Development Program(2016YFA0501304) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; National Natural Science Foundation of China(31570829) ; National Natural Science Foundation of China(31570829) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202)
Language英语
WOS Research AreaBiochemistry & Molecular Biology
WOS SubjectBiochemical Research Methods
WOS KeywordHISTAMINE-RELEASING FACTOR ; COLD-SHOCK DOMAIN ; Y-BOX PROTEINS ; IN-VIVO ; THERAPEUTIC TARGET ; YB-1 ; PROLIFERATION ; GROWTH ; ACTIVATION ; BREAST
WOS IDWOS:000385054100026
Funding OrganizationNational Key Research and Development Program(2016YFA0501304) ; National Key Research and Development Program(2016YFA0501304) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; National Natural Science Foundation of China(31570829) ; National Natural Science Foundation of China(31570829) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202) ; National Key Research and Development Program(2016YFA0501304) ; National Key Research and Development Program(2016YFA0501304) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; State Key Laboratory of Freshwater Ecology and Biotechnology(2015FB10) ; National Natural Science Foundation of China(31570829) ; National Natural Science Foundation of China(31570829) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202) ; Strategic Priority Research Program of the Chinese Academy of Sciences(XDB14030202)
Citation statistics
Document Type期刊论文
Identifierhttp://ir.ihb.ac.cn/handle/342005/28566
Collection藻类生物学及应用研究中心_水生生物分子与细胞生物学研究中心
Affiliation1.Chinese Acad Sci, Wuhan Inst Virol, Inst Hydrobiol, Key Lab Algal Biol, Wuhan 430072, Peoples R China
2.Chinese Acad Sci, Wuhan Inst Virol, State Key Lab Virol, Wuhan 430072, Peoples R China
3.Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China
Recommended Citation
GB/T 7714
Li, Siting,Chen, Minghai,Xiong, Qian,et al. Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells[J]. JOURNAL OF PROTEOME RESEARCH,2016,15(10):3741-3751.
APA Li, Siting,Chen, Minghai,Xiong, Qian,Zhang, Jia,Cui, Zongqiang,&Ge, Feng.(2016).Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells.JOURNAL OF PROTEOME RESEARCH,15(10),3741-3751.
MLA Li, Siting,et al."Characterization of the Translationally Controlled Tumor Protein (TCTP) Interactome Reveals Novel Binding Partners in Human Cancer Cells".JOURNAL OF PROTEOME RESEARCH 15.10(2016):3741-3751.
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