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学科主题: 物理化学
题名: A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis
作者: Wang, Xu1, 2;  Bian, Yangyang3;  Cheng, Kai3;  Gu, Li-Fei1, 2;  Ye, Mingliang3;  Zou, Hanfa3;  Sun, Samuel Sai-Ming1, 2;  He, Jun-Xian1, 2
通讯作者: 邹汉法 ;  SamuelSaiMingSun ;  JunXianHe
关键词: Protein phosphorylation ;  Phosphoproteomics ;  Phosphorylation motif ;  Ti4+-IMAC ;  Arabidopsis thaliana
刊名: JOURNAL OF PROTEOMICS
发表日期: 2013-01-14
DOI: 10.1016/j.jprot.2012.10.018
卷: 78, 页:486-498
收录类别: SCI
文章类型: Article
部门归属: 18
项目归属: 1809
产权排名: 2,2
WOS标题词: Science & Technology ;  Life Sciences & Biomedicine
类目[WOS]: Biochemical Research Methods
研究领域[WOS]: Biochemistry & Molecular Biology
英文摘要: Large-scale protein phosphorylation analysis by MS is emerging as a powerful tool in plant signal transduction research. However, our current understanding of the phosphorylation regulatory network in plants is still very limited. Here, we report on a proteome-wide profiling of phosphopeptides in nine-day-old Arabidopsis (Arabidopsis thaliana) seedlings by using an enrichment method combining the titanium (Ti4+)-based IMAC and the RP-strong cation exchange (RP-SCX) biphasic trap column-based online RPLC. Through the duplicated RPLC-MS/MS analyses, we identified 5348 unique phosphopeptides for 2552 unique proteins. Among the phosphoproteins identified, 41% of them were first-time identified. Further evolutionary conservation and phosphorylation motif analyses of the phosphorylation sites discovered 100 highly conserved phosphorylation residues and identified 17 known and 14 novel motifs specific for Ser/Thr protein kinases. Gene ontology and pathway analyses revealed that many of the new identified phosphoproteins are important regulatory proteins that are involved in diverse biological processes, particularly in central metabolisms and cell signaling. Taken together, our results provided not only new insights into the complex phosphoregulatory network in plants but also important resources for future functional studies of protein phosphorylation in plant growth and development. (C) 2012 Elsevier B.V. All rights reserved.
关键词[WOS]: BRASSINOSTEROID SIGNAL-TRANSDUCTION ;  PHOSPHOPROTEOME PROFILING REVEALS ;  ION AFFINITY-CHROMATOGRAPHY ;  HIGH-THROUGHPUT ;  QUANTITATIVE PHOSPHOPROTEOMICS ;  MULTIDIMENSIONAL SEPARATION ;  BIOLOGICAL NETWORKS ;  SEQUENCE ALIGNMENT ;  PROTEOMIC ANALYSIS ;  GENE ONTOLOGY
语种: 英语
WOS记录号: WOS:000316706800037
Citation statistics: 
内容类型: 期刊论文
URI标识: http://cas-ir.dicp.ac.cn/handle/321008/117523
Appears in Collections:中国科学院大连化学物理研究所_期刊论文

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作者单位: 1.Chinese Univ Hong Kong, State Key Lab Agrobiotechnol, Shatin, Hong Kong, Peoples R China
2.Chinese Univ Hong Kong, Sch Life Sci, Shatin, Hong Kong, Peoples R China
3.Chinese Acad Sci, Key Lab Separat Sci Analyt Chem, Natl Chromatog R&A Ctr, Dalian Inst Chem Phys, Dalian 116023, Peoples R China

Recommended Citation:
Wang, Xu,Bian, Yangyang,Cheng, Kai,et al. A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis[J]. JOURNAL OF PROTEOMICS,2013,78:486-498.
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