Activation of an atypical plant NLR with an N-terminal deletion initiates cell 
death at the vacuole

Sunil, S; Beeh, S; Stöbbe, E; Fischer, K; Wilhelm, F; Meral, A; Paris, C; Teasdale, L; Jiang, Z; Zhang, L; Urban, M; Aguilar Parras, E; Nürnberger, T; Weigel, D; Lozano-Duran, R; El Kasmi, F

doi:10.1038/s44319-024-00240-4

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Activation of an atypical plant NLR with an N-terminal deletion initiates cell death at the vacuole

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Teasdale, L
Department Molecular Biology, Max Planck Institute for Biology Tübingen, Max Planck Society;

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Weigel, D
Department Molecular Biology, Max Planck Institute for Biology Tübingen, Max Planck Society;

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Citation

Sunil, S., Beeh, S., Stöbbe, E., Fischer, K., Wilhelm, F., Meral, A., et al. (2024). Activation of an atypical plant NLR with an N-terminal deletion initiates cell death at the vacuole. EMBO Reports, 25(10), 4358-4386. doi:10.1038/s44319-024-00240-4.

Cite as: https://hdl.handle.net/21.11116/0000-000F-D720-A

Abstract

Plants evolve nucleotide-binding leucine-rich repeat receptors (NLRs) to induce immunity. Activated coiled-coil (CC) domain containing NLRs (CNLs) oligomerize and form apparent cation channels promoting calcium influx and cell death, with the alpha-1 helix of the individual CC domains penetrating the plasma membranes. Some CNLs are characterized by putative N-myristoylation and S-acylation sites in their CC domain, potentially mediating permanent membrane association. Whether activated Potentially Membrane Localized NLRs (PMLs) mediate cell death and calcium influx in a similar way is unknown. We uncovered the cell-death function at the vacuole of an atypical but conserved Arabidopsis PML, PML5, which has a significant deletion in its CCG10/GA domain. Active PML5 oligomers localize in Golgi membranes and the tonoplast, alter vacuolar morphology, and induce cell death, with the short N-terminus being sufficient. Mutant analysis supports a potential role of PMLs in plant immunity. PML5-like deletions are found in several Brassicales paralogs, pointing to the evolutionary importance of this innovation. PML5, with its minimal CC domain, represents the first identified CNL utilizing vacuolar-stored calcium for cell death induction.