Release of a ubiquitin brake activates OsCERK1-triggered immunity in rice.
Nature
; 629(8014): 1158-1164, 2024 May.
Article
en En
| MEDLINE
| ID: mdl-38750355
ABSTRACT
Plant pattern-recognition receptors perceive microorganism-associated molecular patterns to activate immune signalling1,2. 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 autoimmunity3,4. 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.
Texto completo:
1
Banco de datos:
MEDLINE
Asunto principal:
Proteínas de Plantas
/
Oryza
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Ubiquitina
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Inmunidad de la Planta
Límite:
Animals
Idioma:
En
Revista:
Nature
/
Nature (Lond.)
/
Nature (London)
Año:
2024
Tipo del documento:
Article
País de afiliación:
China