Journal
JOURNAL OF PROTEOMICS
Volume 78, Issue -, Pages 486-498Publisher
ELSEVIER
DOI: 10.1016/j.jprot.2012.10.018
Keywords
Protein phosphorylation; Phosphoproteomics; Phosphorylation motif; Ti4+-IMAC; Arabidopsis thaliana
Categories
Funding
- Hong Kong RGC General Research Fund (CUHK) [465009, 465410]
- National Natural Science Foundation of China [91125027]
- Chinese University of Hong Kong
- Creative Research Group Project of NSFC [21021004]
- National Transgenic Project of China [2009ZX08009-001b]
- Hong Kong UGC AoE Center for Plant and Agricultural Biotechnology Project [AoE-B-07/09]
- Resource Allocation Committee, The Chinese University of Hong Kong
- China State Key Basic Research Program Grant [2012CB910601]
- Analytical Method Innovation Program of MOST [2009IM031800]
Ask authors/readers for more resources
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.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available