ArticleThe New phytologist2025
Redox regulation of LSD1/CATALASE 2 phase separation condensates controls location and functions.
Article in The New phytologist, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- A redox-regulated RCC1-like protein controls catalase activity in Arabidopsis.Nature communications · 2026Article
- Reactive oxygen species and oxidative signalling in plants.Essays in biochemistry · 2026Review
- Visualisation of peroxisomes: a journey through seven decades.Histochemistry and cell biology · 2026Review
- Biomolecular Condensates in Combined and Recurrent Plant Stresses: Integrating Phase Separation, Signal Prioritization, and Cross-Stress Memory.International journal of molecular sciences · 2026Review
- Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Emerging concepts of reactive oxygen species functions in plants.Biochemical Society transactions · 2026Review
- Transcriptomic identification of potential antioxidative enzyme regulators of the gametophytic-to-embryogenic switch in barley microspores.Frontiers in plant science · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Phase separation of proteins into membraneless compartments is emerging as an important mechanism of plant developmental and stress responses. We show Arabidopsis catalase 2 (CAT2) is recruited to phase-separated condensates with LESION SIMULATING DISEASE1 (LSD1), a plant-specific regulator of programmed cell death, in a redox-dependent manner that regulates its intracellular localisation and activity. Using recombinant proteins, we showed that CAT2 and LSD1 form ternary complexes with the peroxisome import receptor PEX5. The ability of LSD1 to form phase-separated condensates is a property of zinc fingers 1 and 2. The interactions between all three proteins and the fluidity of the LSD1 condensates are redox-regulated. Using confocal microscopy, the in vivo trafficking of CAT2 to peroxisomes and the nuclei was shown to be redox-regulated, and LSD1 was shown to control CAT2 localisation in vivo. We propose a model whereby the redox-dependent differential accessibility of CAT2, PEX5 and LSD1 within condensates not only regulates CAT2 activity but also compartmentalisation between peroxisome, cytosol and nucleus. Relocation of catalase to the nucleus may provide protection to nuclear processes under conditions of biotic stress.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.