Publication Information
Yang et al., 2013
No external accession available
Abstract
Mol Cell Proteomics. 2013 Dec;12(12):3559-82. doi: 10.1074/mcp.M113.031633. Epub
2013 Sep 16.
Stable isotope metabolic labeling-based quantitative phosphoproteomic analysis
of Arabidopsis mutants reveals ethylene-regulated time-dependent phosphoproteins
and putative substrates of constitutive triple response 1 kinase.
Yang Z(1), Guo G, Zhang M, Liu CY, Hu Q, Lam H, Cheng H, Xue Y, Li J, Li N.
Author information:
(1)Division of Life Science, The Hong Kong University of Science and Technology,
Hong Kong SAR, China;
Ethylene is an important plant hormone that regulates numerous cellular
processes and stress responses. The mode of action of ethylene is both dose- and
time-dependent. Protein phosphorylation plays a key role in ethylene signaling,
which is mediated by the activities of ethylene receptors, constitutive triple
response 1 (CTR1) kinase, and phosphatase. To address how ethylene alters the
cellular protein phosphorylation profile in a time-dependent manner,
differential and quantitative phosphoproteomics based on (15)N stable isotope
labeling in Arabidopsis was performed on both one-minute ethylene-treated
Arabidopsis ethylene-overly-sensitive loss-of-function mutant rcn1-1, deficient
in PP2A phosphatase activity, and a pair of long-term ethylene-treated wild-type
and loss-of-function ethylene signaling ctr1-1 mutants, deficient in
mitogen-activated kinase kinase kinase activity. In total, 1079 phosphopeptides
were identified, among which 44 were novel. Several one-minute
ethylene-regulated phosphoproteins were found from the rcn1-1. Bioinformatic
analysis of the rcn1-1 phosphoproteome predicted nine phosphoproteins as the
putative substrates for PP2A phosphatase. In addition, from CTR1 kinase-enhanced
phosphosites, we also found putative CTR1 kinase substrates including plastid
transcriptionally active protein and calcium-sensing receptor. These regulatory
proteins are phosphorylated in the presence of ethylene. Analysis of
ethylene-regulated phosphosites using the group-based prediction system with a
protein-protein interaction filter revealed a total of 14 kinase-substrate
relationships that may function in both CTR1 kinase- and PP2A
phosphatase-mediated phosphor-relay pathways. Finally, several
ethylene-regulated post-translational modification network models have been
built using molecular systems biology tools. It is proposed that ethylene
regulates the phosphorylation of arginine/serine-rich splicing factor 41, plasma
membrane intrinsic protein 2A, light harvesting chlorophyll A/B binding protein
1.1, and flowering bHLH 3 proteins in a dual-and-opposing fashion.
DOI: 10.1074/mcp.M113.031633
PMCID: PMC3861708
PMID: 24043427 [Indexed for MEDLINE]
