中国科学院机构知识库网格
Chinese Academy of Sciences Institutional Repositories Grid
A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis

文献类型:期刊论文

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
刊名journal of proteomics
出版日期2013-01-14
卷号78页码:486-498
关键词Protein phosphorylation Phosphoproteomics Phosphorylation motif Ti4+-IMAC Arabidopsis thaliana
ISSN号1874-3919
产权排序2,2
通讯作者邹汉法 ; samuelsaimingsun ; junxianhe
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.
WOS标题词science & technology ; life sciences & biomedicine
学科主题物理化学
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
收录类别SCI
语种英语
WOS记录号WOS:000316706800037
公开日期2013-10-11
源URL[http://159.226.238.44/handle/321008/117523]  
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
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
推荐引用方式
GB/T 7714
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.,...&He, Jun-Xian.(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.

入库方式: OAI收割

来源:大连化学物理研究所

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