Functional phosphoproteomic profiling of phosphorylation sites in membrane fractions of salt-stressed Arabidopsis thaliana

in Sciences Citation Index(SCI), 科學引文索引資料庫(SCI)
標題Functional phosphoproteomic profiling of phosphorylation sites in membrane fractions of salt-stressed Arabidopsis thaliana
出版類型SCI(Sciences Citation Index)
AuthorsLiao Ming-Huei, 徐睿良, Lan-Yu Wang 王蘭玉, Shu-Ying Wang 王舒瑩, Ching-Huang Lin 林靖凰, Kuo-Chieh Ho 何國傑, Fong-Ku Shi 石峰鵠, & Ing-Feng Chang 張英峰
出版日期2009 / 11
其他編號NSC 98-2113-M-020 -002 -MY2

Background: Under conditions of salt stress, plants respond by initiating phosphorylation
cascades. Many key phosphorylation events occur at the membrane. However, to date only limited
sites have been identified that are phosphorylated in response to salt stress in plants.
Results: Membrane fractions from three-day and 200 mM salt-treated Arabidopsis suspension
plants were isolated, followed by protease shaving and enrichment using Zirconium ion-charged
magnetic beads, and tandem mass spectrometry analyses. From this isolation, 18 phosphorylation
sites from 15 Arabidopsis proteins were identified. A unique phosphorylation site in 14-3-3-
interacting protein AHA1 was predominately identified in 200 mM salt-treated plants. We also
identified some phosphorylation sites in aquaporins. A doubly phosphorylated peptide of PIP2;1 as
well as a phosphopeptide containing a single phosphorylation site (Ser-283) and a phosphopeptide
containing another site (Ser-286) of aquaporin PIP2;4 were identified respectively. These two sites
appeared to be novel of which were not reported before. In addition, quantitative analyses of
protein phosphorylation with either label-free or stable-isotope labeling were also employed in this
study. The results indicated that level of phosphopeptides on five membrane proteins such as
AHA1, STP1, Patellin-2, probable inactive receptor kinase (At3g02880), and probable purine
permease 18 showed at least two-fold increase in comparison to control in response to 200 mM
Conclusion: In this study, we successfully identified novel salt stress-responsive protein
phosphorylation sites from membrane isolates of abiotic-stressed plants by membrane shaving
followed by Zr4+-IMAC enrichment. The identified phosphorylation sites can be important in the
salt stress response in plants.

期刊名稱Proteome Science
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