Arabidopsis ADR1 helper NLR immune receptors localize and function at the plasma membrane in a phospholipid dependent manner

© 2021 The Authors New Phytologist © 2021 New Phytologist Foundation.

Bibliographische Detailangaben
Veröffentlicht in:The New phytologist. - 1979. - 232(2021), 6 vom: 10. Dez., Seite 2440-2456
1. Verfasser: Saile, Svenja C (VerfasserIn)
Weitere Verfasser: Ackermann, Frank M, Sunil, Sruthi, Keicher, Jutta, Bayless, Adam, Bonardi, Vera, Wan, Li, Doumane, Mehdi, Stöbbe, Eva, Jaillais, Yvon, Caillaud, Marie-Cécile, Dangl, Jeffery L, Nishimura, Marc T, Oecking, Claudia, El Kasmi, Farid
Format: Online-Aufsatz
Sprache:English
Veröffentlicht: 2021
Zugriff auf das übergeordnete Werk:The New phytologist
Schlagworte:Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S. Arabidopsis thaliana HeLo-/RPW8-type NLRs hypersensitive response-like cell death intracellular localization nucleotide-binding leucine-rich repeat receptors (NLRs) oligomerization mehr... phospholipids plant immunity Arabidopsis Proteins NLR Proteins Phospholipids
Beschreibung
Zusammenfassung:© 2021 The Authors New Phytologist © 2021 New Phytologist Foundation.
Activation of nucleotide-binding leucine-rich repeat receptors (NLRs) results in immunity and a localized cell death. NLR cell death activity requires oligomerization and in some cases plasma membrane (PM) localization. The exact mechanisms underlying PM localization of NLRs lacking predicted transmembrane domains or recognizable lipidation motifs remain elusive. We used confocal microscopy, genetically encoded molecular tools and protein-lipid overlay assays to determine whether PM localization of members of the Arabidopsis HeLo-/RPW8-like domain 'helper' NLR (RNL) family is mediated by the interaction with negatively charged phospholipids of the PM. Our results show that PM localization and stability of some RNLs and one CC-type NLR (CNL) depend on the direct interaction with PM phospholipids. Depletion of phosphatidylinositol-4-phosphate from the PM led to a mis-localization of the analysed NLRs and consequently inhibited their cell death activity. We further demonstrate homo- and hetero-association of members of the RNL family. Our results provide new insights into the molecular mechanism of NLR localization and defines an important role of phospholipids for CNL and RNL PM localization and consequently, for their function. We propose that RNLs interact with anionic PM phospholipids and that RNL-mediated cell death and immune responses happen at the PM
Beschreibung:Date Completed 06.01.2022
Date Revised 31.05.2022
published: Print-Electronic
Citation Status MEDLINE
ISSN:1469-8137
DOI:10.1111/nph.17788