DICP OpenIR
Subject Area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
KeywordProtein Phosphorylation Phosphoproteomics Phosphorylation Motif ti4+-imac Arabidopsis Thaliana
Source PublicationJOURNAL OF PROTEOMICS
2013-01-14
ISSN1874-3919
DOI10.1016/j.jprot.2012.10.018
Volume78Pages:486-498
Indexed BySCI
SubtypeArticle
Department18
Funding Project1809
Contribution Rank2,2
WOS HeadingsScience & Technology ; Life Sciences & Biomedicine
WOS SubjectBiochemical Research Methods
WOS Research AreaBiochemistry & Molecular Biology
WOS KeywordBRASSINOSTEROID SIGNAL-TRANSDUCTION ; PHOSPHOPROTEOME PROFILING REVEALS ; ION AFFINITY-CHROMATOGRAPHY ; HIGH-THROUGHPUT ; QUANTITATIVE PHOSPHOPROTEOMICS ; MULTIDIMENSIONAL SEPARATION ; BIOLOGICAL NETWORKS ; SEQUENCE ALIGNMENT ; PROTEOMIC ANALYSIS ; GENE ONTOLOGY
AbstractLarge-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.
Language英语
WOS IDWOS:000316706800037
Citation statistics
Cited Times:54[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://cas-ir.dicp.ac.cn/handle/321008/117523
Collection中国科学院大连化学物理研究所
Corresponding AuthorZou HF(邹汉法); SamuelSaiMingSun; JunXianHe
Affiliation1.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
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.,...&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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