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学科主题物理化学
A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis
Wang, Xu1,2; Bian, Yangyang3; Cheng, Kai3; Gu, Li-Fei1,2; Ye, Mingliang3; Zou, Hanfa3; Sun, Samuel Sai-Ming1,2; He, Jun-Xian1,2; Zou HF(邹汉法); SamuelSaiMingSun; JunXianHe
关键词Protein Phosphorylation Phosphoproteomics Phosphorylation Motif ti4+-imac Arabidopsis Thaliana
刊名JOURNAL OF PROTEOMICS
2013-01-14
ISSN1874-3919
DOI10.1016/j.jprot.2012.10.018
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
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
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.
语种英语
WOS记录号WOS:000316706800037
引用统计
被引频次:45[WOS]   [WOS记录]     [WOS相关记录]
文献类型期刊论文
条目标识符http://cas-ir.dicp.ac.cn/handle/321008/117523
专题中国科学院大连化学物理研究所
通讯作者Zou HF(邹汉法); SamuelSaiMingSun; JunXianHe
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
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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.
APA Wang, Xu.,Bian, Yangyang.,Cheng, Kai.,Gu, Li-Fei.,Ye, Mingliang.,...&JunXianHe.(2013).A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis.JOURNAL OF PROTEOMICS,78,486-498.
MLA Wang, Xu,et al."A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis".JOURNAL OF PROTEOMICS 78(2013):486-498.
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