Lack of AtMC1 catalytic activity triggers autoimmunity dependent on NLR stability

Plants utilize cell surface-localized pattern recognition receptors (PRRs) and intracellular nucleotide-binding leucine-rich repeat (NLR) receptors to detect non-self and elicit robust immune responses. Fine-tuning the homeostasis of these receptors is critical to prevent their hyperactivation. Here...

Descripción completa

Detalles Bibliográficos
Autores: Salguero-Linares, Jose, Armengot, Laia, Ayet, Joel, Ruiz-Solaní, Neus, Saile, Svenja C., Salas-Gómez, Marta, Fernandez, Esperanza, Denolf, Lode, Navarrete, Fernando, Krumbach, Jenna, Kaiser, Markus, Stael, Simon, Van Breusegem, Frank, Gevaert, Kris, Kaschani, Farnusch, Petersen, Morten, El Kasmi, Farid, Valls Matheu, Marc, Coll, Núria S.
Tipo de recurso: artículo
Estado:Versión publicada
Fecha de publicación:2025
País:España
Institución:Varias* (Consorci de Biblioteques Universitáries de Catalunya, Centre de Serveis Científics i Acadèmics de Catalunya)
Repositorio:Recercat. Dipósit de la Recerca de Catalunya
OAI Identifier:oai:recercat.cat:2445/227203
Acceso en línea:https://hdl.handle.net/2445/227203
Access Level:acceso abierto
Palabra clave:Cèl·lules
Plantes
Autoimmunitat
Cells
Plants
Autoimmunity
Descripción
Sumario:Plants utilize cell surface-localized pattern recognition receptors (PRRs) and intracellular nucleotide-binding leucine-rich repeat (NLR) receptors to detect non-self and elicit robust immune responses. Fine-tuning the homeostasis of these receptors is critical to prevent their hyperactivation. Here, we show that Arabidopsis plants lacking metacaspase 1 (AtMC1) display autoimmunity dependent on immune signalling components downstream of NLR and PRR activation. Overexpression of a catalytically inactive AtMC1 in an atmc1 background triggers severe autoimmunity partially dependent on the same immune signalling components. Overexpression of the E3 ligase SNIPER1, a master regulator of NLR homeostasis, fully reverts the AtMC1-dependent autoimmunity phenotype, inferring that a broad defect in NLR turnover may underlie the severe phenotype observed. Catalytically inactive AtMC1 localizes to punctate structures that are degraded through autophagy. Considering also previous evidence on the proteostatic functions of AtMC1, we speculate that Wt AtMC1 may either directly or indirectly control NLR protein levels, thereby preventing autoimmunity.

Similares en LA Referencia