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BUI1, an actin cytoskeleton protein that confers durable and broad-spectrum resistance in rice

ABSTRACT: The cytoskeleton functions as a dynamic intracellular structural scaffold, enabling cells to rapidly perceive biotic and abiotic stresses. During plant innate immune responses, the cytoskeleton undergoes actin remodeling. Using the rice-Magnaporthe oryzae pathosystem, we investigated changes in actin organization within host plant cells. Our results demonstrate that pattern-triggered immunity (PTI), induced by pathogen-associated molecular patterns (PAMPs), triggers a rapid but transient increase in actin filament abundance. This process depends on BUI1, a type-II formin protein. Disruption of actin filaments with latrunculin B not only suppresses this increase but also enhances host susceptibility. Furthermore, we show that BUI1 positively regulates broad-spectrum resistance against multiple pathogens by suppressing reactive oxygen species (ROS) scavenging. Together, these findings uncover a key mechanism by which receptor-mediated signaling reorganizes the host cytoskeleton during plant-pathogen interactions.

ORGANISM(S): Oryza sativa

PROVIDER: GSE305236 | GEO | 2026/07/08

REPOSITORIES: GEO

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Project description:Plants have evolved a two-layered immune system that mainly includes pattern-triggered immunity (PTI) and effector-triggered immunity (ETI) against pathogen attack. PTI and ETI signaling are functionally linked, but also distinct due to specific perceived ligands and activation modes. Unraveling how PTI and ETI coordinate the immune responses against pathogens is crucial for understanding the regulatory mechanisms in plant immunity. To better understand the protein profiling and phosphorylation events during PTI and ETI, we employed integrated whole proteome and phosphoproteome analyses in the tomato-Pst pathosystem with different Pst DC3000 mutants that allow dissection of different layers of immune responses. A total of 225 proteins and 79 phosphopeptides were differentially regulated in tomato leaves during immune responses. Our proteomics results indicate that some overlapping immune responses are triggered by both PTI and ETI-inducing treatment, and ETI response is more robust than PTI response for most proteins. The change patterns of protein abundance and phosphorylation revealed some key regulators involved in Ca2+ signaling, mitogen-activated protein kinase cascades, and reversible protein phosphorylation, ROS and redox homeostasis, direct defense, transcription machinery and protein turnover, cell wall remodeling, hormone biosynthesis, as well as immune molecule accumulation, are modulated during PTI and/or ETI, suggesting their common or specific roles in plant immune responses. However, NAC domain protein and lipid particle serine esterase, two PTI-specific genes from previous transcriptomic work, have not been detected as differentially regulated in our proteomic analysis, and they were proved to be not PTI-specific inducible and therefore cannot be used as PTI-reporters through “overlapping circle” pattern assay. These results provide insights into the fine-tuned regulatory mechanisms between PTI and ETI in-Pst pathosystem, which will springboard further investigations into the sophisticated mechanisms in plant immunity.

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BUI1, an actin cytoskeleton protein that confers durable and broad-spectrum resistance in rice

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