Sensor NLR immune proteins activate oligomerization of their NRC helpers in response to plant pathogens

Contreras, Mauricio P., Pai, Hsuan, Tumtas, Yasin, Duggan, Cian, Yuen, Enoch Lok Him, Vergara Cruces, Angel, Kourelis, Jiorgos ORCID: https://orcid.org/0000-0002-9007-1333, Ahn, Hee Kyung ORCID: https://orcid.org/0000-0002-8884-0156, Lee, Kim Teng, Wu, Chih Hang, Bozkurt, Tolga O., Derevnina, Lida and Kamoun, Sophien ORCID: https://orcid.org/0000-0002-0290-0315 (2023) Sensor NLR immune proteins activate oligomerization of their NRC helpers in response to plant pathogens. EMBO Journal, 42 (5). ISSN 0261-4189

[thumbnail of Contreras_etal_2022_TheEMBOJournal]
Preview
PDF (Contreras_etal_2022_TheEMBOJournal) - Published Version
Available under License Creative Commons Attribution.

Download (5MB) | Preview

Abstract

Nucleotide-binding domain leucine-rich repeat (NLR) immune receptors are important components of plant and metazoan innate immunity that can function as individual units or as pairs or networks. Upon activation, NLRs form multiprotein complexes termed resistosomes or inflammasomes. Although metazoan paired NLRs, such as NAIP/NLRC4, form hetero-complexes upon activation, the molecular mechanisms underpinning activation of plant paired NLRs, especially whether they associate in resistosome hetero-complexes, is unknown. In asterid plant species, the NLR required for cell death (NRC) immune receptor network is composed of multiple resistance protein sensors and downstream helpers that confer immunity against diverse plant pathogens. Here, we show that pathogen effector-activation of the NLR proteins Rx (confers virus resistance), and Bs2 (confers bacterial resistance) leads to oligomerization of their helper NLR, NRC2. Activated Rx does not oligomerize or enter into a stable complex with the NRC2 oligomer and remains cytoplasmic. In contrast, activated NRC2 oligomers accumulate in membrane-associated puncta. We propose an activation-and-release model for NLRs in the NRC immune receptor network. This points to a distinct activation model compared with mammalian paired NLRs.

Item Type: Article
Additional Information: Acknowledgements: We are very thankful to several colleagues for discussions and ideas. We thank Daniel Lüdke (The Sainsbury Laboratory, Norwich, UK) for valuable comments on this article. We thank all members of the TSL Support Services for their invaluable assistance. We thank S. Hrek. M.C. and S.K. dedicate this article to the memory of Diego A. Maradona. A.V.C. was funded by the John Innes Foundation and TSL. The Kamoun Lab is funded primarily from the Gatsby Charitable Foundation, Biotechnology and Biological Sciences Research Council (BBSRC, UK, BB/WW002221/1, BB/V002937/1, BBS/E/J/000PR9795 and BBS/E/J/000PR9796) and the European Research Council (BLASTOFF). Data availability: All relevant data are within the article, in the Appendix and in the Source Data files. This study includes no data that would need to be deposited in external repositories.
Uncontrolled Keywords: immune receptor,inflammasome,nb-lrr,nod-like receptor,resistosome,neuroscience(all),molecular biology,biochemistry, genetics and molecular biology(all),immunology and microbiology(all) ,/dk/atira/pure/subjectarea/asjc/2800
Faculty \ School: Faculty of Science > The Sainsbury Laboratory
Faculty of Science > School of Biological Sciences
Related URLs:
Depositing User: LivePure Connector
Date Deposited: 07 Dec 2023 01:46
Last Modified: 01 Feb 2024 03:07
URI: https://ueaeprints.uea.ac.uk/id/eprint/93895
DOI: 10.15252/embj.2022111519

Actions (login required)

View Item View Item