細胞死の「美しい」環：ミシガン大学の発見は、生物学的回復力と免疫力に影響を与える(Cell death’s ‘beautiful’ rings: U-M discovery has implications for biological resilience and immunity)

2026-03-12  ミシガン大学

Images from a high resolution microscope at the University of Michigan help reveal a never-before-observed ring structure that researchers have found helps cells mediate the “perfect” amount of cell death. The green parts of the ring show where it is bound to a cell membrane and the red dots are channels that penetrate through the membrane. Image credit: D. Ge et al. Nature, 2026. DOI:10.1038/s41586-026-10215-1 (Used under a Creative Commons license)

＜関連情報＞

• https://news.umich.edu/cell-deaths-beautiful-rings-u-m-discovery-has-implications-for-biological-resilience-and-immunity/
• https://www.nature.com/articles/s41586-026-10215-1

コイルドコイルNLRの活性化に伴うヘルパーNLRレジストソームクラスターの集合 Assembly of helper NLR resistosome clusters upon activation of a coiled-coil NLR

Dongdong Ge,Fausto Andres Ortiz-Morea,Yingpeng Xie,In-Cheol Yeo,Qiaochu Shen,Yulu Zhou,Guangchao Liu,Liang Kong,Libo Shan & Ping He
Nature  Published:11 March 2026
DOI:https://doi.org/10.1038/s41586-026-10215-1

Abstract

Plant nucleotide-binding leucine-rich repeat (NLR) immune receptors detect pathogen effectors and activate immunity¹. Coiled-coil NLRs (CNLs) form resistosomes as Ca²⁺-permeable channels in the plasma membrane (PM)^2,3,4. However, the mechanism by which resistosomes activate cell death remains unclear. Here we report that the CNL SUPPRESSOR OF mkk1 mkk2 2 (SUMM2), unlike canonical CNLs that use a MADA motif to penetrate the PM⁵, tethers to the PM through N-myristoylation, a common feature among many CNLs. PM targeting via N-myristoylation is essential for SUMM2-induced cell death. Upon activation, SUMM2 promotes the association of the lipase-like proteins ENHANCED DISEASE SUSCEPTIBILITY 1 (EDS1) and PHYTOALEXIN DEFICIENT 4 (PAD4) with the helper NLR-ACTIVATED DISEASE RESISTANCE 1-LIKE 1 (ADR1-L1). Furthermore, active SUMM2 induces the clustering of multiple ADR1-L1 resistosomes into a ring-like assembly colocalized with the EDS1–PAD4 complex, and the EDS1–PAD4–ADR1 module is essential for SUMM2-activated cell death. Together, these findings reveal that N-myristoylation-mediated PM targeting of SUMM2 promotes the assembly of higher-order EDS1–PAD4–ADR1-L1 resistosome clusters for cell death initiation.