Proteomic analysis reveals novel molecules involved in insulin signaling pathway
文献类型：期刊论文
| 作者 | Wang, YG; Li, RX; Du, D; Zhang, CY; Yuan, HX; Zeng, R; Chen, ZJ |
| 刊名 | JOURNAL OF PROTEOME RESEARCH
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| 出版日期 | 2006 |
| 卷号 | 5期号:4页码:846-855 |
| 关键词 | insulin signaling pathway subcellular fractionation immuno-affinity purification phosphotyrosine sites CASK T-element |
| 通讯作者 | Chen, ZJ (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Biochem & Cell Biol,Res Ctr Proteome Anal, Key Lab Proteom,SHARF Lab, 320 Yue Yang Rd, Shanghai 200031, Peoples R China.,zr@sibs.ac.cn ; zjchen@sibs.ac.cn |
| 英文摘要 | The binding of insulin to its receptor triggers a signaling cascade regulated by protein complexes via tyrosine phosphorylation events on a multitude of associated proteins. To search novel phosphotyrosine proteins or associated proteins involved in insulin signaling pathway, we employed a method in which Rat1 cells stably expressing the human insulin receptor were stimulated with or without insulin and sub-fractionated prior to enrichment of phosphotyrosine proteins by immunoprecipitation and analysis by LC-MS/MS. Bioinformatic analysis and manual confirmation of peptide phosphorylation site assignments led to identification of 35 phosphotyrosine sites derived from 31 protein groups. Over 50% of these proteins were reported for the first time as tyrosine phosphorylated, including gigaxonin, XIAP and CDK10. In addition, we also found that calcium/calmodulin-dependent protein serine kinase (CASK), a key protein in protein-targeting and vesicle transport in neurons, forms a complex with two unidentified phosphotyrosine proteins pp100 and pp95 in response to insulin-stimulation, though CASK is not itself tyrosine phosphorylated. Furthermore, insulin was able to decrease CASK nuclear location, as well as down-regulate the expression of CASK targeted genes. Our results imply CASK as a novel joint knot connecting CASK-mediated pathways with the insulin signaling. Our data provide a wealth of information potentially paving the way to identify new components in the insulin signaling network. |
| 学科主题 | Biochemistry & Molecular Biology |
| 类目[WOS] | Biochemical Research Methods |
| 关键词[WOS] | MASS-SPECTROMETRY ; GROWTH-FACTOR ; TYROSINE PHOSPHORYLATION ; QUANTITATIVE PROTEOMICS ; DOMAIN INTERACTIONS ; 3T3-L1 ADIPOCYTES ; BRAIN-DEVELOPMENT ; PLASMA-MEMBRANE ; PROTEIN COMPLEX ; KINASE-ACTIVITY |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000236816100014 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/1706]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Wang, YG,Li, RX,Du, D,et al. Proteomic analysis reveals novel molecules involved in insulin signaling pathway[J]. JOURNAL OF PROTEOME RESEARCH,2006,5(4):846-855. |
| APA | Wang, YG.,Li, RX.,Du, D.,Zhang, CY.,Yuan, HX.,...&Chen, ZJ.(2006).Proteomic analysis reveals novel molecules involved in insulin signaling pathway.JOURNAL OF PROTEOME RESEARCH,5(4),846-855. |
| MLA | Wang, YG,et al."Proteomic analysis reveals novel molecules involved in insulin signaling pathway".JOURNAL OF PROTEOME RESEARCH 5.4(2006):846-855. |
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