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Publication Abstract from PubMed

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.

Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice.,Wang G, Chen X, Yu C, Shi X, Lan W, Gao C, Yang J, Dai H, Zhang X, Zhang H, Zhao B, Xie Q, Yu N, He Z, Zhang Y, Wang E Nature. 2024 May 15. doi: 10.1038/s41586-024-07418-9. PMID:38750355^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.