Stable Isotope Metabolic Labeling-based Quantitative Phosphoproteomic Analysis of Arabidopsis Mutants Reveals Ethylene-regulated Time-dependent Phosphoproteins and Putative Substrates of Constitutive Triple Response 1 Kinase
文献类型：期刊论文
| 作者 | Yang, Zhu5; Guo, Guangyu5; Zhang, Manyu5; Liu, Claire Y.5; Hu, Qin5; Lam, Henry6; Cheng, Han7; Xue, Yu7; Li, Jiayang8,9; Li, Ning5 |
| 刊名 | MOLECULAR & CELLULAR PROTEOMICS
 |
| 出版日期 | 2013-12-01 |
| 卷号 | 12期号:12页码:3559-3582 |
| ISSN号 | 1535-9476 |
| DOI | 10.1074/mcp.M113.031633 |
| 英文摘要 | Ethylene is an important plant hormone that regulates numerous cellular processes and stress responses. The mode of action of ethylene is both dose- and time-dependent. Protein phosphorylation plays a key role in ethylene signaling, which is mediated by the activities of ethylene receptors, constitutive triple response 1 (CTR1) kinase, and phosphatase. To address how ethylene alters the cellular protein phosphorylation profile in a time-dependent manner, differential and quantitative phosphoproteomics based on N-15 stable isotope labeling in Arabidopsis was performed on both one-minute ethylene-treated Arabidopsis ethylene-overly-sensitive loss-of-function mutant rcn1-1, deficient in PP2A phosphatase activity, and a pair of long-term ethylene-treated wild-type and loss-of-function ethylene signaling ctr1-1 mutants, deficient in mitogen-activated kinase kinase kinase activity. In total, 1079 phosphopeptides were identified, among which 44 were novel. Several one-minute ethylene-regulated phosphoproteins were found from the rcn1-1. Bioinformatic analysis of the rcn1-1 phosphoproteome predicted nine phosphoproteins as the putative substrates for PP2A phosphatase. In addition, from CTR1 kinase-enhanced phosphosites, we also found putative CTR1 kinase substrates including plastid transcriptionally active protein and calcium-sensing receptor. These regulatory proteins are phosphorylated in the presence of ethylene. Analysis of ethylene-regulated phosphosites using the group-based prediction system with a protein-protein interaction filter revealed a total of 14 kinase-substrate relationships that may function in both CTR1 kinase- and PP2A phosphatase-mediated phosphor-relay pathways. Finally, several ethylene-regulated post-translational modification network models have been built using molecular systems biology tools. It is proposed that ethylene regulates the phosphorylation of arginine/serine-rich splicing factor 41, plasma membrane intrinsic protein 2A, light harvesting chlorophyll A/B binding protein 1.1, and flowering bHLH 3 proteins in a dual-and-opposing fashion. |
| 语种 | 英语 |
| 出版者 | AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC |
| WOS记录号 | WOS:000329993600012 |
| 源URL | [http://ir.iccas.ac.cn/handle/121111/43319]  |
| 专题 | 中国科学院化学研究所 |
| 通讯作者 | Li, Ning |
| 作者单位 | 1.Hong Kong Univ Sci & Technol, Div Life Sci, Hong Kong, Peoples R China 2.Hong Kong Univ Sci & Technol, Dept Chem & Biomol Engn, Hong Kong, Peoples R China 3.Huazhong Univ Sci & Technol, Dept Biomed Engn, Coll Life Sci & Technol, Wuhan 430074, Hunan, Peoples R China 4.Chinese Acad Sci, Inst Genet & Dev Biol, State Key Lab Plant Genom & Natl Ctr Plant Gene R, Beijing 100101, Peoples R China 5.Hong Kong Univ Sci & Technol, Div Life Sci, Hong Kong, Hong Kong, Peoples R China 6.Hong Kong Univ Sci & Technol, Dept Chem & Biomol Engn, Hong Kong, Hong Kong, Peoples R China 7.Huazhong Univ Sci & Technol, Coll Life Sci & Technol, Dept Biomed Engn, Wuhan 430074, Hubei, Peoples R China 8.Chinese Acad Sci, State Key Lab Plant Genom, Beijing 100101, Peoples R China 9.Chinese Acad Sci, Natl Ctr Plant Gene Res, Inst Genet & Dev Biol, Beijing 100101, Peoples R China |
| 推荐引用方式 GB/T 7714 | Yang, Zhu,Guo, Guangyu,Zhang, Manyu,et al. Stable Isotope Metabolic Labeling-based Quantitative Phosphoproteomic Analysis of Arabidopsis Mutants Reveals Ethylene-regulated Time-dependent Phosphoproteins and Putative Substrates of Constitutive Triple Response 1 Kinase[J]. MOLECULAR & CELLULAR PROTEOMICS,2013,12(12):3559-3582. |
| APA | Yang, Zhu.,Guo, Guangyu.,Zhang, Manyu.,Liu, Claire Y..,Hu, Qin.,...&Li, Ning.(2013).Stable Isotope Metabolic Labeling-based Quantitative Phosphoproteomic Analysis of Arabidopsis Mutants Reveals Ethylene-regulated Time-dependent Phosphoproteins and Putative Substrates of Constitutive Triple Response 1 Kinase.MOLECULAR & CELLULAR PROTEOMICS,12(12),3559-3582. |
| MLA | Yang, Zhu,et al."Stable Isotope Metabolic Labeling-based Quantitative Phosphoproteomic Analysis of Arabidopsis Mutants Reveals Ethylene-regulated Time-dependent Phosphoproteins and Putative Substrates of Constitutive Triple Response 1 Kinase".MOLECULAR & CELLULAR PROTEOMICS 12.12(2013):3559-3582. |
入库方式： OAI收割
来源：化学研究所
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。