ArticleProceedings of the National Academy of Sciences of the United States of America2016
Luminidependens (LD) is an Arabidopsis protein with prion behavior.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 90 papers.
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Who cites it
90 citing papers in PubMed.
- Aspects of plant intelligence (ii).Plant signaling & behavior · 2026Review
- Sensing and Filtering Environmental Fluctuations: The Case of Biomolecular Condensates in Plants.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026Review
- Transcriptomic analysis of Rnq1 loss and prionization reveals alterations in translation pathways and energy metabolism.Scientific reports · 2026Article
- Molecular basis for thermoresponsive protein condensation in plants.bioRxiv : the preprint server for biology · 2025Article
- The prion-like characteristic of ORF3 contributes to virion release and pathogenesis of hepatitis E virus.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- A Prion-Like Domain in EBV EBNA1 Promotes Phase Separation and Enables SRRM1 Splicing.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Leveraging structure-informed machine learning for fast steric zipper propensity prediction across whole proteomes.PLoS computational biology · 2025Article
- Phase Separation: Orchestrating Biological Adaptations to Environmental Fluctuations.International journal of molecular sciences · 2025Review
- Modular in vivo assembly of Arabidopsis FCA oligomers into condensates competent for RNA 3' processing.The EMBO journal · 2025Article
- Genome-wide identification and analysis of the UBA2 gene family in wheat (Triticum aestivum L.).BMC genomics · 2025Article
- Investigating the Aggregation and Prionogenic Properties of Human Cancer-Related Proteins.Molecular and cellular biology · 2025Article
- Prion-like Proteins in Plants: Key Regulators of Development and Environmental Adaptation via Phase Separation.Plants (Basel, Switzerland) · 2024Review
- A prion-like domain is required for phase separation and chloroplast RNA processing during cold acclimation in Arabidopsis.The Plant cell · 2024Article
- In silico analysis of fungal prion-like proteins for elucidating their role in plant-fungi interactions.Archives of microbiology · 2024Article
- Physiology of Cellular Prion Proteins in Reproduction.Development & reproduction · 2024Article
- Article
- Heat stress promotes Arabidopsis AGO1 phase separation and association with stress granule components.iScience · 2024Article
- Biomolecular condensation orchestrates clathrin-mediated endocytosis in plants.Nature cell biology · 2024Article
- Liquid-liquid phase separation in plants: Advances and perspectives from model species to crops.Plant communications · 2024Review
- Roles of prion proteins in mammalian development.Animal cells and systems · 2024Review
30 more citing papers are in PubMed but not listed here.
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6 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Prion proteins provide a unique mode of biochemical memory through self-perpetuating changes in protein conformation and function. They have been studied in fungi and mammals, but not yet identified in plants. Using a computational model, we identified candidate prion domains (PrDs) in nearly 500 plant proteins. Plant flowering is of particular interest with respect to biological memory, because its regulation involves remembering and integrating previously experienced environmental conditions. We investigated the prion-forming capacity of three prion candidates involved in flowering using a yeast model, where prion attributes are well defined and readily tested. In yeast, prions heritably change protein functions by templating monomers into higher-order assemblies. For most yeast prions, the capacity to convert into a prion resides in a distinct prion domain. Thus, new prion-forming domains can be identified by functional complementation of a known prion domain. The prion-like domains (PrDs) of all three of the tested proteins formed higher-order oligomers. Uniquely, the Luminidependens PrD (LDPrD) fully replaced the prion-domain functions of a well-characterized yeast prion, Sup35. Our results suggest that prion-like conformational switches are evolutionarily conserved and might function in a wide variety of normal biological processes.
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