Oxygen-evolving enhancer protein 2 is phosphorylated by glycine-rich protein 3/wall-associated kinase 1 in Arabidopsis

Eun Ju Yang, Young Ah Oh, Eui Seung Lee, Ae Ran Park, Somi K. Cho, Yung Joon Yoo, Ohkmae Kim

Research output: Contribution to journalArticle

46 Citations (Scopus)


The Arabidopsis wall-associated receptor kinase, WAK1, is a member of WAK family that links the plasma membrane to the extracellular matrix. A glycine-rich secreted protein, AtGRP-3, was previously shown to regulate WAK1 functions through binding to the extracellular domain of WAK1. In this study, we sought to determine the downstream molecules of the AtGRP-3/WAK1 signaling pathway, by using two-dimensional gel electrophoresis combined with Edman sequencing and matrix-assisted laser desorption/ionization-time-of-flight mass spectrometry (MALDI-TOF MS). We report here that a chloroplast protein, oxygen-evolving enhancer protein 2 (OEE2), specifically interacts with the cytoplasmic kinase domain of WAK1 and becomes phosphorylated in an AtGRP-3-dependent manner. The phosphorylation of OEE2 is also induced in Arabidopsis by treatment with avirulent Pseudomonas syringae. Taken together, these results suggest that OEE2 activity is regulated by AtGRP-3/WAK1.

Original languageEnglish
Pages (from-to)862-868
Number of pages7
JournalBiochemical and Biophysical Research Communications
Issue number4
Publication statusPublished - 2003 Jun 13
Externally publishedYes



  • Arabidopsis
  • AtGRP-3
  • Kinase
  • OEE2
  • Receptor
  • Signal transduction
  • WAK1

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

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