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The phosphoproteome of Arabidopsis plants lacking the oxidative signal‐inducible1 (OXI1) protein kinase
Author(s) -
Howden Andrew J.M.,
Salek Mogjiborahman,
Miguet Laurent,
Pullen Margaret,
Thomas Benjamin,
Knight Marc R.,
Sweetlove Lee J.
Publication year - 2011
Publication title -
new phytologist
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 3.742
H-Index - 244
eISSN - 1469-8137
pISSN - 0028-646X
DOI - 10.1111/j.1469-8137.2010.03582.x
Subject(s) - biology , protein phosphorylation , biochemistry , phosphorylation , phosphoprotein , microbiology and biotechnology , signal transduction , protein kinase a , arabidopsis , kinase , arabidopsis thaliana , proteome , mutant , gene
Summary• The AGC protein kinase OXI1 is a key protein in plant responses to oxidative signals, and is important for two oxidative burst‐mediated processes: basal resistance to microbial pathogens and root hair growth. To identify possible components of the OXI1 signalling pathway, phosphoproteomic techniques were used to detect alterations in the abundance of phosphorylated proteins and peptides in an oxi1 null mutant of Arabidopsis thaliana . • The relative abundance of phosphorylated proteins was assessed either using two‐dimensional gel electrophoresis and staining with the phosphoprotein stain Pro‐Q Diamond or by the identification and quantification, by mass spectrometry, of stable‐isotope labelled phosphopeptides. • A number of proteins show altered phosphorylation in the oxi1 mutant. Five proteins, including a putative F‐box and 3‐phosphoinositide‐dependent kinase 1, show reduced phosphorylation in the oxi1 mutant, and may be direct or indirect targets of OXI1. Four proteins, including ethylene insensitive 2 and phospholipase d ‐gamma, show increased phosphorylation in the oxi1 mutant. • This study has identified a range of candidate proteins from the OXI1 signalling pathway. The diverse activities of these proteins, including protein degradation and hormone signalling, may suggest crosstalk between OXI1 and other signal transduction cascades.