Publication Information
Rayapuram et al., 2014
No external accession available
Abstract
J Proteome Res. 2014 Apr 4;13(4):2137-51. doi: 10.1021/pr401268v. Epub 2014 Mar
17.
Identification of novel PAMP-triggered phosphorylation and dephosphorylation
events in Arabidopsis thaliana by quantitative phosphoproteomic analysis.
Rayapuram N(1), Bonhomme L, Bigeard J, Haddadou K, Przybylski C, Hirt H,
Pflieger D.
Author information:
(1)CNRS, UMR 8587, boulevard François Mitterrand, 91025 Evry, France.
Signaling cascades rely strongly on protein kinase-mediated substrate
phosphorylation. Currently a major challenge in signal transduction research is
to obtain high confidence substrate phosphorylation sites and assign them to
specific kinases. In response to bacterial flagellin, a pathogen-associated
molecular pattern (PAMP), we searched for rapidly phosphorylated proteins in
Arabidopsis thaliana by combining multistage activation (MSA) and electron
transfer dissociation (ETD) fragmentation modes, which generate complementary
spectra and identify phosphopeptide sites with increased reliability. Of a total
of 825 phosphopeptides, we identified 58 to be differentially phosphorylated.
These peptides harbor kinase motifs of mitogen-activated protein kinases (MAPKs)
and calcium-dependent protein kinases (CDPKs), as well as yet unknown protein
kinases. Importantly, 12 of the phosphopeptides show reduced phosphorylation
upon flagellin treatment. Since protein abundance levels did not change, these
results indicate that flagellin induces not only various protein kinases but
also protein phosphatases, even though a scenario of inhibited kinase activity
may also be possible.
DOI: 10.1021/pr401268v
PMID: 24601666 [Indexed for MEDLINE]
