{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Jacob P"],"funding":["UKRI | Biotechnology and Biological Sciences Research Council","National Science Foundation (NSF)","Biotechnology and Biological Sciences Research Council","National Science Foundation"],"pagination":["e2220921120"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC10242710"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["120(11)"],"pubmed_abstract":["TIR domains are NAD-degrading enzymes that function during immune signaling in prokaryotes, plants, and animals. In plants, most TIR domains are incorporated into intracellular immune receptors termed TNLs. In Arabidopsis, TIR-derived small molecules bind and activate EDS1 heterodimers, which in turn activate RNLs, a class of cation channel-forming immune receptors. RNL activation drives cytoplasmic Ca<sup>2+</sup> influx, transcriptional reprogramming, pathogen resistance, and host cell death. We screened for mutants that suppress an RNL activation mimic allele and identified a TNL, SADR1. Despite being required for the function of an autoactivated RNL, SADR1 is not required for defense signaling triggered by other tested TNLs. SADR1 is required for defense signaling initiated by some tra"],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pubmed_title":["Broader functions of TIR domains in Arabidopsis immunity."],"pmcid":["PMC10242710"],"funding_grant_id":["BB/V01627X/1","BB/R000689/1","IOS-1758400"],"pubmed_authors":["McKinney BJ","Nishimura MT","Wunsch L","Grant MR","Bayless A","Song L","Dangl JL","Russ D","Yang Y","Jacob P","El Kasmi F","Fitzpatrick CR","Hige J","Bonardi V"],"additional_accession":[]},"is_claimable":false,"name":"Broader functions of TIR domains in Arabidopsis immunity.","description":"TIR domains are NAD-degrading enzymes that function during immune signaling in prokaryotes, plants, and animals. In plants, most TIR domains are incorporated into intracellular immune receptors termed TNLs. In Arabidopsis, TIR-derived small molecules bind and activate EDS1 heterodimers, which in turn activate RNLs, a class of cation channel-forming immune receptors. RNL activation drives cytoplasmic Ca<sup>2+</sup> influx, transcriptional reprogramming, pathogen resistance, and host cell death. We screened for mutants that suppress an RNL activation mimic allele and identified a TNL, SADR1. Despite being required for the function of an autoactivated RNL, SADR1 is not required for defense signaling triggered by other tested TNLs. SADR1 is required for defense signaling initiated by some tra","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Mar","modification":"2026-05-28T19:56:41.341Z","creation":"2025-02-19T02:38:03.485Z"},"accession":"S-EPMC10242710","cross_references":{"pubmed":["36893276"],"doi":["10.1073/pnas.2220921120"]}}