Large-scale phosphorylation mapping reveals the extent of tyrosine phosphorylation in Arabidopsis

Naoyuki Sugiyama, Hirofumi Nakagami, Keiichi Mochida, Arsalan Daudi, Masaru Tomita, Ken Shirasu, Yasushi Ishihama

Research output: Contribution to journalArticlepeer-review

327 Citations (Scopus)


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.

Original languageEnglish
Article number193
JournalMolecular Systems Biology
Publication statusPublished - 2008
Externally publishedYes


  • Arabidopsis
  • Phosphoproteome
  • Tyrosine kinase
  • Tyrosine phosphorylation

ASJC Scopus subject areas

  • General Biochemistry,Genetics and Molecular Biology
  • General Immunology and Microbiology
  • General Agricultural and Biological Sciences
  • Applied Mathematics


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