Autophosphorylation site Y428 is essential for the in vivo activation of CERK1

Plant Signal Behav. 2018 Feb 1;13(2):e1435228. doi: 10.1080/15592324.2018.1435228. Epub 2018 Feb 20.

Abstract

Autophosphorylation of PRR is a critical event for the activation of immune signaling in plant. However, the detailed function of these phosphorylation sites is still not well understood. We analyzed the function of an autophosphorylation site of Arabidopsis CERK1, Y428, in immune signaling. Biochemical characterization of CERK1 mutants transiently expressed in N. benthamiana indicated that Y428 plays a crucial role for the in vivo activation of CERK1, differently from the previous observation by the in vitro kinase assay with its cytoplasmic domain. Similar discrepancy between in vitro and in vivo kinase assay was also reported for the corresponding phosphorylation site of EFR, suggesting that these conserved tyrosine residues play important roles for the activation of both RD and non-RD RLKs.

Keywords: Arabidopsis; CERK1; Nicotiana benthamiana; PRR; RLK; phosphorylation site; phosphotyrosine.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Arabidopsis / genetics
  • Arabidopsis / metabolism
  • Nicotiana / genetics
  • Nicotiana / metabolism*
  • Phosphorylation
  • Protein Serine-Threonine Kinases / genetics
  • Protein Serine-Threonine Kinases / metabolism*

Substances

  • Protein Serine-Threonine Kinases

Grants and funding

This work was supported in part by Grants-in-Aid for Scientific Research (26650104 to N.S.) and Grants-in-Aid for Scientific Research on Innovative Areas (25114516 to N.S. and15H01240 to H.K.), MEXT-Supported Program for the Strategic Research Foundation at Private Universities 2014–2018 (S1411023) from MEXT, Japan to H.K.