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Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice.

Gang WangXi ChenChengzhi YuXiaobao ShiWenxian LanChaofeng GaoJun YangHuiling DaiXiaowei ZhangHuili ZhangBoyu ZhaoReetika DebroyNan YuZuhua HeYu ZhangErtao Wang
Published in: Nature (2024)
Plant pattern-recognition receptors perceive microorganism-associated molecular patterns to activate immune signalling 1,2 . Activation of the pattern-recognition receptor kinase CERK1 is essential for immunity, but tight inhibition of receptor kinases in the absence of pathogen is crucial to prevent autoimmunity 3,4 . Here we find that the U-box ubiquitin E3 ligase OsCIE1 acts as a molecular brake to inhibit OsCERK1 in rice. During homeostasis, OsCIE1 ubiquitinates OsCERK1, reducing its kinase activity. In the presence of the microorganism-associated molecular pattern chitin, active OsCERK1 phosphorylates OsCIE1 and blocks its E3 ligase activity, thus releasing the brake and promoting immunity. Phosphorylation of a serine within the U-box of OsCIE1 prevents its interaction with E2 ubiquitin-conjugating enzymes and serves as a phosphorylation switch. This phosphorylation site is conserved in E3 ligases from plants to animals. Our work identifies a ligand-released brake that enables dynamic immune regulation.
Keyphrases
  • protein kinase
  • transcription factor
  • small molecule
  • binding protein
  • single molecule
  • blood brain barrier
  • tyrosine kinase
  • gene expression
  • dna methylation
  • mouse model
  • candida albicans
  • celiac disease