Foerderer, Alexander, Yu, Dongli ORCID: 0000-0001-9258-8435, Li, Ertong and Chai, Jijie (2022). Resistosomes at the interface of pathogens and plants. Curr. Opin. Plant Biol., 67. LONDON: CURRENT BIOLOGY LTD. ISSN 1879-0356

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Abstract

Nucleotide-binding and leucine-rich repeat (NLR) proteins are a large family of intracellular immune receptors that detect specific pathogen effector proteins secreted into plant cells. Upon direct or indirect recognition of effector proteins, NLRs form higher-order oligomeric complexes termed resistosomes that trigger defence responses typically associated with a regulated cell death. Here, we review recent advances in our understanding of signalling mediated by plant NLR resisto-somes. Emphasis is placed on discussing the activation mechanisms and biochemical functions of resistosomes. We also summarize the most recent research in structure-based rational engineering of NLRs. At the end, we outline chal-lenging questions concerning the elucidation of resistosome signalling.

Item Type: Journal Article
Creators:
CreatorsEmailORCIDORCID Put Code
Foerderer, AlexanderUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Yu, DongliUNSPECIFIEDorcid.org/0000-0001-9258-8435UNSPECIFIED
Li, ErtongUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
Chai, JijieUNSPECIFIEDUNSPECIFIEDUNSPECIFIED
URN: urn:nbn:de:hbz:38-672166
DOI: 10.1016/j.pbi.2022.102212
Journal or Publication Title: Curr. Opin. Plant Biol.
Volume: 67
Date: 2022
Publisher: CURRENT BIOLOGY LTD
Place of Publication: LONDON
ISSN: 1879-0356
Language: English
Faculty: Unspecified
Divisions: Unspecified
Subjects: no entry
Uncontrolled Keywords:
KeywordsLanguage
RUST RESISTANCE PROTEIN; NBS-LRR PROTEIN; IMMUNE RECEPTORS; CELL-DEATH; CRYSTAL-STRUCTURE; SELF-ASSOCIATION; STRUCTURAL BASIS; TIR DOMAINS; ARC DOMAIN; REVEALSMultiple languages
Plant SciencesMultiple languages
URI: http://kups.ub.uni-koeln.de/id/eprint/67216

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