Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder
文献类型：期刊论文
| 作者 | Liu, Xuguang2; Bian, Yangyang1,6; Li, Lei2,3; Dong, Mingming1,6; Kaneko, Tomonori2; Cheng, Kai6; Liu, Huadong2; Voss, Courtney2; Cao, Xuan2; Wang, Yan |
| 刊名 | NATURE CHEMICAL BIOLOGY
 |
| 出版日期 | 2016-11-01 |
| 卷号 | 12期号:11页码:959-+ |
| ISSN号 | 1552-4450 |
| DOI | 10.1038/NCHEMBIO.2178 |
| 文献子类 | Article |
| 英文摘要 | We present a new strategy for systematic identification of phosphotyrosine (pTyr) by affinity purification mass spectrometry (AP-MS) using a Src homology 2 (SH2)-domain-derived pTyr superbinder as the affinity reagent. The superbinder allows for markedly deeper coverage of the Tyr phosphoproteome than anti-pTyr antibodies when an optimal amount is used. We identified similar to 20,000 distinct phosphotyrosyl peptides and >10,000 pTyr sites, of which 36% were 'novel', from nine human cell lines using the superbinder approach. Tyrosine kinases, SH2 domains and phosphotyrosine phosphatases were preferably phosphorylated, suggesting that the toolkit of kinase signaling is subject to intensive regulation by phosphorylation. Cell-type-specific global kinase activation patterns inferred from label-free quantitation of Tyr phosphorylation guided the design of experiments to inhibit cancer cell proliferation by blocking the highly activated tyrosine kinases. Therefore, the superbinder is a highly efficient and cost-effective alternative to conventional antibodies for systematic and quantitative characterization of the tyrosine phosphoproteome under normal or pathological conditions. |
| WOS关键词 | ION AFFINITY-CHROMATOGRAPHY ; BREAST-CANCER CELLS ; FACTOR-I RECEPTOR ; POSTTRANSLATIONAL MODIFICATIONS ; PHOSPHORYLATION DYNAMICS ; SIGNALING NETWORKS ; MASS-SPECTROMETRY ; ACTIVATION LOOP ; HUMAN PROTEOME ; LUNG-CANCER |
| WOS研究方向 | Biochemistry & Molecular Biology |
| 语种 | 英语 |
| WOS记录号 | WOS:000386798800018 |
| 出版者 | NATURE PUBLISHING GROUP |
| 源URL | [http://cas-ir.dicp.ac.cn/handle/321008/169894]  |
| 专题 | 大连化学物理研究所_中国科学院大连化学物理研究所 |
| 通讯作者 | Ye, Mingliang; Li, Shawn S-C; Zou, Hanfa |
| 作者单位 | 1.Univ Chinese Acad Sci, Beijing, Peoples R China 2.Western Univ, Dept Biochem, Schulich Sch Med & Dent, London, ON, Canada 3.Qingdao Univ, Sch Basic Med Sci, Qingdao, Peoples R China 4.Western Univ, Schulich Sch Med & Dent, Childrens Hlth Res Inst, London, ON, Canada 5.Western Univ, Schulich Sch Med & Dent, Dept Oncol, London, ON, Canada 6.Chinese Acad Sci, Dalian Inst Chem Phys, Natl Chromatog R&D Ctr, Key Lab Separat Sci Analyt Chem, Dalian, Peoples R China |
| 推荐引用方式 GB/T 7714 | Liu, Xuguang,Bian, Yangyang,Li, Lei,et al. Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder[J]. NATURE CHEMICAL BIOLOGY,2016,12(11):959-+. |
| APA | Liu, Xuguang.,Bian, Yangyang.,Li, Lei.,Dong, Mingming.,Kaneko, Tomonori.,...&Zou, Hanfa.(2016).Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder.NATURE CHEMICAL BIOLOGY,12(11),959-+. |
| MLA | Liu, Xuguang,et al."Ultra-deep tyrosine phosphoproteomics enabled by a phosphotyrosine superbinder".NATURE CHEMICAL BIOLOGY 12.11(2016):959-+. |
入库方式： OAI收割
来源：大连化学物理研究所
浏览0
下载0
收藏0
其他版本
除非特别说明，本系统中所有内容都受版权保护，并保留所有权利。