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• W2548564213 abstract "Plants and animals use intracellular innate immune receptors known as nucleotide-binding oligomerization domain-like receptors (NLRs) to detect the presence of pathogens and activate defense. Although genetic studies have defined an increasing number of receptors and the pathogen triggers that activate them, the structural and mechanistic underpinnings of the events at, and downstream of, perception have lagged behind. There are no full-length structures available for NLRs, so researchers have had to content themselves with partial structures, often individual domains. The functional relevance of these partial structures can be difficult to parse. Nevertheless, in a pair of articles in PNAS, Cesari et al. (1) and Casey et al. (2) have provided a clearer view into exactly how NLR proteins function.Microbes become pathogens by defeating some aspect of the host immune system. Plant pathogens from all kingdoms have evolved a set of molecular tools: protein virulence effectors that are delivered into the host cytoplasm. Once inside the host, pathogen effectors target a variety of host processes to promote virulence. These targets can be conserved aspects of the immune system, or can be more specialized targets with pathogen-specific outcomes (3, 4). Plant genomes have responded by evolving specific NLRs that recognize the presence of pathogen virulence effectors and respond appropriately to defeat pathogens (often with programmed cell death) (5). A detailed structural and mechanistic understanding of exactly how NLR proteins respond to pathogens is critical for ensuring food security by rationally engineering disease resistance in crops. We need to know both how the immune response is suppressed in the absence of pathogens and how it is appropriately activated.Models of NLR immune function are informed by their multidomain architecture. In plants, NLRs are characterized by three domains: ( i ) an N-terminal coiled-coil (CC) or Toll/interleukin-1 receptor (TIR) domain, ( ii ) a central nucleotide-binding (NB) … [↵][1]1To whom correspondence should be addressed. Email: marcusn{at}colostate.edu. [1]: #xref-corresp-1-1" @default.
• W2548564213 created "2016-11-11" @default.
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• W2548564213 date "2016-11-01" @default.
• W2548564213 modified "2023-09-24" @default.
• W2548564213 title "Structural insights into plant NLR immune receptor function" @default.
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• W2548564213 doi "https://doi.org/10.1073/pnas.1615933113" @default.
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