Publication Information
Wang et al., 2013
No external accession available
Abstract
J Proteomics. 2013 Jan 14;78:486-98. doi: 10.1016/j.jprot.2012.10.018. Epub 2012
Oct 27.
A large-scale protein phosphorylation analysis reveals novel phosphorylation
motifs and phosphoregulatory networks in Arabidopsis.
Wang X(1), Bian Y, Cheng K, Gu LF, Ye M, Zou H, Sun SS, He JX.
Author information:
(1)State Key Laboratory of Agrobiotechnology and School of Life Sciences, The
Chinese University of Hong Kong, Shatin, NT, Hong Kong SAR, China.
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 (Ti(4+))-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.
Copyright © 2012 Elsevier B.V. All rights reserved.
DOI: 10.1016/j.jprot.2012.10.018
PMID: 23111157 [Indexed for MEDLINE]
