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      TIR signal promotes interactions between lipase-like proteins and ADR1-L1 receptor and ADR1-L1 oligomerization

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          Abstract

          TIR signaling promotes the interactions between lipase-like proteins EDS1/PAD4 and ADR1-L1 immune receptor, and oligomerization of ADR1-L1.

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          Intracellular innate immune surveillance devices in plants and animals.

          Jonathan Jones, Russell E Vance, Jeffery Dangl (2016)
          Multicellular eukaryotes coevolve with microbial pathogens, which exert strong selective pressure on the immune systems of their hosts. Plants and animals use intracellular proteins of the nucleotide-binding domain, leucine-rich repeat (NLR) superfamily to detect many types of microbial pathogens. The NLR domain architecture likely evolved independently and convergently in each kingdom, and the molecular mechanisms of pathogen detection by plant and animal NLRs have long been considered to be distinct. However, microbial recognition mechanisms overlap, and it is now possible to discern important key trans-kingdom principles of NLR-dependent immune function. Here, we attempt to articulate these principles. We propose that the NLR architecture has evolved for pathogen-sensing in diverse organisms because of its utility as a tightly folded "hair trigger" device into which a virtually limitless number of microbial detection platforms can be integrated. Recent findings suggest means to rationally design novel recognition capabilities to counter disease.
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            The ZAR1 resistosome is a calcium-permeable channel triggering plant immune signaling

            Guozhi Bi, Min Su, Nan Li … (2021)
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              NAD+ cleavage activity by animal and plant TIR domains in cell death pathways

              Shane Horsefield, Hayden Burdett, Xiaoxiao Zhang … (2019)
              SARM1 (sterile alpha and TIR motif containing 1) is responsible for depletion of nicotinamide adenine dinucleotide in its oxidized form (NAD + ) during Wallerian degeneration associated with neuropathies. Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors recognize pathogen effector proteins and trigger localized cell death to restrict pathogen infection. Both processes depend on closely related Toll/interleukin-1 receptor (TIR) domains in these proteins, which, as we show, feature self-association–dependent NAD + cleavage activity associated with cell death signaling. We further show that SARM1 SAM (sterile alpha motif) domains form an octamer essential for axon degeneration that contributes to TIR domain enzymatic activity. The crystal structures of ribose and NADP + (the oxidized form of nicotinamide adenine dinucleotide phosphate) complexes of SARM1 and plant NLR RUN1 TIR domains, respectively, reveal a conserved substrate binding site. NAD + cleavage by TIR domains is therefore a conserved feature of animal and plant cell death signaling pathways.
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                Author and article information

                Journal
                Journal ID (nlm-ta): Plant Physiol
                Journal ID (iso-abbrev): Plant Physiol
                Journal ID (publisher-id): plphys
                Title: Plant Physiology
                Publisher: Oxford University Press
                ISSN (Print): 0032-0889
                ISSN (Electronic): 1532-2548
                Publication date Collection: October 2021
                Publication date (Electronic): 02 July 2021
                Publication date PMC-release: 02 July 2021
                Volume: 187
                Issue: 2
                Pages: 681-686
                Affiliations
                [1 ] Michael Smith Laboratories, Department of Botany, University of British Columbia , Vancouver, BC, Canada V6T 1Z4
                [2 ] Department of Botany, University of British Columbia , Vancouver, BC, Canada V6T 1Z4
                Author notes
                Author for communication: xinli@ 123456msl.ubc.ca
                [†]

                Senior author.

                [‡]

                These authors contributed equally to this work.

                Author information
                https://orcid.org/0000-0001-6687-1675
                https://orcid.org/0000-0002-9395-7762
                https://orcid.org/0000-0002-7413-4947
                https://orcid.org/0000-0002-3480-5478
                https://orcid.org/0000-0002-6354-2021
                Article
                Publisher ID: kiab305
                DOI: 10.1093/plphys/kiab305
                PMC ID: 8491023
                PubMed ID: 34608964
                SO-VID: 687f3a57-861a-456a-80a1-604305ebecbd
                Copyright © © The Author(s) 2021. Published by Oxford University Press on behalf of American Society of Plant Biologists.
                License:

                This is an Open Access article distributed under the terms of the Creative Commons Attribution License ( https://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

                History
                Date received : 16 April 2021
                Date accepted : 05 June 2021
                Page count
                Pages: 6
                Funding
                Funded by: CFI-JELF, the Natural Sciences and Engineering Research Council of Canada (NSERC) Discovery Program;
                Funded by: NSERC-CREATE PRoTECT program;
                Funded by: China Scholarship Council (CSC);
                Categories
                Subject: Regular Issue
                Subject: Letter
                Subject: Signaling and Response
                Subject: AcademicSubjects/SCI02286
                Subject: AcademicSubjects/SCI02287
                Subject: AcademicSubjects/SCI01270
                Subject: AcademicSubjects/SCI01280
                Subject: AcademicSubjects/SCI02288

                ScienceOpen disciplines: Plant science & Botany
                Data availability:
                ScienceOpen disciplines: Plant science & Botany

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