| Autor: |
Sunil, Sruthi, Beeh, Simon, Stöbbe, Eva, Fischer, Kathrin, Wilhelm, Franziska, Meral, Aron, Paris, Celia, Teasdale, Luisa, Jiang, Zhihao, Zhang, Lisha, Urban, Moritz, Aguilar Parras, Emmanuel, Nürnberger, Thorsten, Weigel, Detlef, Lozano-Duran, Rosa, El Kasmi, Farid |
| Zdroj: |
EMBO Reports; Oct2024, Vol. 25 Issue 10, p4358-4386, 29p |
| Abstrakt: |
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. Synopsis: An atypical plant NLR immune receptor with a conserved N-terminal deletion initiates cell-death potentially by forming resistosomes at the vacuolar membrane, leading to cytosolic calcium influx and vacuolar fragmentation. PML5 is a CCG10-type coiled-coil (CC) domain containing NLR (CNL) with a conserved N-terminal deletion. PML5 allows conclusions to be drawn about the minimal structural requirements for cell death initiation. PML5 localizes to Golgi and vacuolar membranes. PML5 may form resistosomes at the tonoplast to initiate cytosolic calcium influx, vacuolar fragmentation, and cell death. An atypical plant NLR immune receptor with a conserved N-terminal deletion initiates cell-death potentially by forming resistosomes at the vacuolar membrane, leading to cytosolic calcium influx and vacuolar fragmentation. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Complementary Index |
| Externí odkaz: |
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