Autophosphorylation of Specific Threonine and Tyrosine Residues in Arabidopsis CERK1 is Essential for the Activation of Chitin-Induced Immune Signaling

Plant Cell Physiol. 2016 Nov;57(11):2312-2322. doi: 10.1093/pcp/pcw150. Epub 2016 Aug 26.


Pattern recognition receptors on the plant cell surface mediate the recognition of microbe/damage-associated molecular patterns (MAMPs/DAMPs) and activate downstream immune signaling. Autophosphorylation of signaling receptor-like kinases is a critical event for the activation of downstream responses but the function of each phosphorylation site in the regulation of immune signaling is not well understood. In this study, 41 Ser/Thr/Tyr and 15 Ser/Thr residues were identified as in vitro and in vivo autophosphorylation sites of Arabidopsis CERK1, which is essential for chitin signaling. Comprehensive analysis of transgenic plants expressing mutated CERK1 genes for each phosphorylation site in the cerk1-2 background indicated that the phosphorylation of T479 in the activation segment and Y428 located upstream of the catalytic loop is important for the activation of chitin-triggered defense responses. Contribution of the phosphorylation of T573 to the chitin responses was also suggested. In vitro evaluation of kinase activities of mutated kinase domains indicated that the phosphorylation of T479 and T573 is directly involved in the regulation of kinase activity of CERK1 but the phosphorylation of Y428 regulates chitin signaling independently of the regulation of kinase activity. These results indicated that the phosphorylation of specific residues in the kinase domain contributes to the regulation of downstream signaling either through the regulation of kinase activity or the different mechanisms, e.g. regulation of protein-protein interactions.

Keywords: Arabidopsis thaliana; CERK1; Chitin; PRR; Phosphorylation site; Plant immunity; Signal transduction.

MeSH terms

  • Amino Acid Sequence
  • Arabidopsis / enzymology*
  • Arabidopsis / immunology*
  • Arabidopsis Proteins / chemistry*
  • Arabidopsis Proteins / metabolism*
  • Chitin / pharmacology*
  • Mutation
  • Phosphorylation / drug effects
  • Plant Immunity / drug effects
  • Plants, Genetically Modified
  • Protein Domains
  • Protein Serine-Threonine Kinases / chemistry*
  • Protein Serine-Threonine Kinases / metabolism*
  • Signal Transduction* / drug effects
  • Threonine / metabolism*
  • Tyrosine / metabolism*


  • Arabidopsis Proteins
  • Chitin
  • Threonine
  • Tyrosine
  • CERK1 protein, Arabidopsis
  • Protein Serine-Threonine Kinases