A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis

	A large-scale protein phosphorylation analysis reveals novel phosphorylation motifs and phosphoregulatory networks in Arabidopsis
	Wang, Xu 1,2; Bian, Yangyang 3; Cheng, Kai 3; Gu, Li-Fei 1,2; Ye, Mingliang 3; Zou, Hanfa 3; Sun, Samuel Sai-Ming 1,2; He, Jun-Xian 1,2
刊名	journal of proteomics
	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
通讯作者	邹汉法 ; samuelsaimingsun ; junxianhe
产权排序	2,2
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.
学科主题	物理化学
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
收录类别	SCI
语种	英语
WOS记录号	WOS:000316706800037
公开日期	2013-10-11
内容类型	期刊论文
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.