Publication Information
Chen et al., 2010
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Abstract
Plant J. 2010 Jul 1;63(1):1-17. doi: 10.1111/j.1365-313X.2010.04218.x. Epub 2010
Mar 31.
Comparative analysis of phytohormone-responsive phosphoproteins in Arabidopsis
thaliana using TiO2-phosphopeptide enrichment and mass accuracy precursor
alignment.
Chen Y(1), Hoehenwarter W, Weckwerth W.
Author information:
(1)Max Planck Institute of Molecular Plant Physiology, Am Mühlenberg 1, 14476,
Potsdam-Golm, Germany.
Protein phosphorylation/dephosphorylation is a central post-translational
modification in plant hormone signaling, but little is known about its extent
and function. Although pertinent protein kinases and phosphatases have been
predicted and identified for a variety of hormone responses, classical
biochemical approaches have so far revealed only a few candidate proteins and
even fewer phosphorylation sites. Here we performed a global quantitative
analysis of the Arabidopsis phosphoproteome in response to a time course of
treatments with various plant hormones using phosphopeptide enrichment and
subsequent mass accuracy precursor alignment (MAPA). The use of three time
points, 1, 3 and 6 h, in combination with five phytohormone treatments, abscisic
acid (ABA), indole-3-acetic acid (IAA), gibberellic acid (GA), jasmonic acid
(JA) and kinetin, resulted in 324,000 precursor ions from 54 LC-Orbitrap-MS
analyses quantified and aligned in a data matrix with the dimension of 6000 x 54
using the ProtMax algorithm. To dissect the phytohormone responses, multivariate
principal/independent components analysis was performed. In total, 152
phosphopeptides were identified as differentially regulated; these
phosphopeptides are involved in a wide variety of signaling pathways. New
phosphorylation sites were identified for ABA response element binding factors
that showed a specific increase in response to ABA. New phosphorylation sites
were also found for RLKs and auxin transporters. We found that different
hormones regulate distinct amino acid residues of members of the same protein
families. In contrast, tyrosine phosphorylation of the G alpha subunit appeared
to be a common response for multiple hormones, demonstrating global cross-talk
among hormone signaling pathways.
DOI: 10.1111/j.1365-313X.2010.04218.x
PMID: 20374526 [Indexed for MEDLINE]
