Publication Information
Sugiyama et al., 2008
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Abstract
Mol Syst Biol. 2008;4:193. doi: 10.1038/msb.2008.32. Epub 2008 May 6.
Large-scale phosphorylation mapping reveals the extent of tyrosine
phosphorylation in Arabidopsis.
Sugiyama N(1), Nakagami H, Mochida K, Daudi A, Tomita M, Shirasu K, Ishihama Y.
Author information:
(1)Institute for Advanced Biosciences, Keio University, Tsuruoka, Japan.
Protein phosphorylation regulates a wide range of cellular processes. Here, we
report the proteome-wide mapping of in vivo phosphorylation sites in Arabidopsis
by using complementary phosphopeptide enrichment techniques coupled with
high-accuracy mass spectrometry. Using unfractionated whole cell lysates of
Arabidopsis, we identified 2597 phosphopeptides with 2172 high-confidence,
unique phosphorylation sites from 1346 proteins. The distribution of
phosphoserine, phosphothreonine, and phosphotyrosine sites was 85.0, 10.7, and
4.3%. Although typical tyrosine-specific protein kinases are absent in
Arabidopsis, the proportion of phosphotyrosines among the phospho-residues in
Arabidopsis is similar to that in humans, where over 90 tyrosine-specific
protein kinases have been identified. In addition, the tyrosine phosphoproteome
shows features distinct from those of the serine and threonine phosphoproteomes.
Taken together, we highlight the extent and contribution of tyrosine
phosphorylation in plants.
DOI: 10.1038/msb.2008.32
PMCID: PMC2424297
PMID: 18463617 [Indexed for MEDLINE]
