Assembly and functional mechanisms of plant NLR resistosomes.

Abstract

Nucleotide-binding and leucine-rich repeat (NLR) proteins are essential intracellular immune receptors in both animal and plant kingdoms. Sensing of pathogen-derived signals induces oligomerization of NLR proteins, culminating in the formation of higher-order protein complexes known as resistosomes in plants. The NLR resistosomes play a pivotal role in mediating the plant immune response against invading pathogens. Over the past few years, our understanding of NLR biology has significantly advanced, particularly in the structural and biochemical aspects of the NLR resistosomes. Here, we highlight the recent advancements in the structural knowledge of how NLR resistosomes are activated and assembled, and how the structural knowledge provides insights into the biochemical functions of these NLR resistosomes, which converge on Ca²⁺ signals. Signaling mechanisms of the resistosomes that underpin plant immunity are also briefly discussed.