Concentrating and sequestering biomolecules in condensates: impact on plant biology

Mountourakis, Fanourios; Hatzianestis, Ioannis H.; Stavridou, Stella; Bozhkov, Peter V.; Moschou, Panagiotis N.

doi:10.1093/jxb/erac497

Cited by 6 publications

(3 citation statements)

References 21 publications

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“…The authors employed an ATP biosensor fused to p33 or an LLPS‐deficient mutant to illustrate the crucial role of vir‐condensate formation in maintaining optimal local ATP production. Lin & Nagy's findings nicely complement previous literature that demonstrated that cellular condensates concentrate biomolecules and increase the efficiency of biochemical reactions (Mountourakis et al ., 2023). In summary, viral condensates may enhance virus fitness by facilitating the concentration of biomolecules, thereby improving the efficiency of energy‐intensive processes such as RNA replication.…”

Section: Figmentioning

confidence: 99%

Plant viruses and biomolecular condensates: novel perspectives in virus replication strategies

May

2024

New Phytologist

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Biomolecular condensates are dynamic, membraneless, cellular compartments formed by the reversible assembly of proteins, nucleic acids, and other biomolecules (Hyman et al., 2014). The functions of these condensates in cellular processes have been extensively studied in mammalian systems (Yoshizawa et al., 2020), but similar studies in plants have traditionally lagged far behind. However, in the past c. 5 years, a flurry of research in plants has revealed that biomolecular condensates play crucial roles in cellular organization and functions. These functions are wide-ranging and include flowering, stress responses, RNA processing, and DNA damage, among others (Liu et al., 2024). Like cellular proteins, viral proteins can form condensates during infection, contributing significantly to virus replication cycles. While the functions of biomolecular condensates formed by viral pathogens in mammals are well-documented (Zhang et al., 2023), our understanding of the functions of condensates formed by plant viruses is limited. In an article published in this issue of New Phytologist, Lin & Nagy (2024; 1917-1935 demonstrate that biomolecular condensates formed during Tomato bushy stunt virus (TBSV, Tombusviridae family) infection sequester glycolytic enzymes and increase local adenosine triphosphate (ATP) concentrations for virus replication. These findings advance our understanding of the pro-viral roles of biomolecular condensates, broadening possibilities for how plant viruses concentrate biomolecules beyond traditional membrane-bound virus inclusions formed during infection.

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Section: Figmentioning

confidence: 99%

Plant viruses and biomolecular condensates: novel perspectives in virus replication strategies

May

2024

New Phytologist

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“…In the model plant, Arabidopsis (Arabidopsis thaliana) LLPS condensates are involved in, for example, the internal chloroplast cargo sorting, transcriptional circuits modulating defence, RNA processing, and temperature sensing [6][7][8][9][10]. Furthermore, plants form conserved condensates like stress granules and processing bodies [11][12][13]. Recent evidence suggests that like their animal counterparts, plant condensates can interface with membranes.…”

Section: Introductionmentioning

confidence: 99%

SEC14-like condensate phase transitions at plasma membranes regulate root growth in Arabidopsis

Liu,

Mentzelopoulou,

Papagavriil

et al. 2023

PLoS Biol

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Protein function can be modulated by phase transitions in their material properties, which can range from liquid- to solid-like; yet, the mechanisms that drive these transitions and whether they are important for physiology are still unknown. In the model plant Arabidopsis, we show that developmental robustness is reinforced by phase transitions of the plasma membrane-bound lipid-binding protein SEC14-like. Using imaging, genetics, and in vitro reconstitution experiments, we show that SEC14-like undergoes liquid-like phase separation in the root stem cells. Outside the stem cell niche, SEC14-like associates with the caspase-like protease separase and conserved microtubule motors at unique polar plasma membrane interfaces. In these interfaces, SEC14-like undergoes processing by separase, which promotes its liquid-to-solid transition. This transition is important for root development, as lines expressing an uncleavable SEC14-like variant or mutants of separase and associated microtubule motors show similar developmental phenotypes. Furthermore, the processed and solidified but not the liquid form of SEC14-like interacts with and regulates the polarity of the auxin efflux carrier PINFORMED2. This work demonstrates that robust development can involve liquid-to-solid transitions mediated by proteolysis at unique plasma membrane interfaces.

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“…In the model plant, Arabidopsis (Arabidopsis thaliana) LLPS is involved in, for example, the internal chloroplast cargo sorting, defence, diurnal rhythms, RNA processing, and environmental sensing by forming plant-specific condensates [6][7][8][9][10]. Furthermore, plants form stress granules and processing bodies to sense and respond to environmental stimuli [11][12][13]. Condensates of the TPLATE, a plant-specific complex involved in endocytosis can likely form on the plasma membrane [14].…”

Section: Introductionmentioning

confidence: 99%

Phase transitions of a SEC14-like condensate at Arabidopsis plasma membranes regulate root growth

Liu

Mentzelopoulou

Deli

et al. 2022

Preprint

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Robust development can be modulated by local protein accumulation which is sometimes manifested as polarity patterns; yet, the mechanisms that lead to these patterns are largely unknown. Using the model plant Arabidopsis, we report that auxin-induced polar patterns can be reinforced by the phase transition of a SEC14-like lipid-binding protein at the plasma membrane. Using imaging, genetics, and in vitro reconstitutions, we show that the SEC14-like phase transition is promoted outside the stem cell root niche through its association with the caspase-like protease separase and conserved microtubule motors in a plasma membrane interface. Separase cleaves SEC14-like to promote its transition from liquid-like clusters to solid-like filaments. Filaments self-amplify and potentiate the robustness and maintenance of plasma membrane domains through associations with polar proteins. This work uncovers that robust cell patterns involve proteolysis-mediated phase transitions at unpreceded plasma membrane interfaces.

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Concentrating and sequestering biomolecules in condensates: impact on plant biology

Abstract: Growing examples of protein condensation phenomena prompt the re-evaluation of their functions in cells.We hereby discuss the possible implications of protein condensation for plant biology.

Cited by 6 publications

References 21 publications

Plant viruses and biomolecular condensates: novel perspectives in virus replication strategies

Plant viruses and biomolecular condensates: novel perspectives in virus replication strategies

SEC14-like condensate phase transitions at plasma membranes regulate root growth in Arabidopsis

Phase transitions of a SEC14-like condensate at Arabidopsis plasma membranes regulate root growth

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