ReviewPlant physiology2026
Twenty-five years of photobodies: formation, composition, and the 2-compartment logic of phytochrome B signaling.
Review in Plant physiology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
1 citing paper in PubMed.
- Phytochrome B sets condensate number through graded nucleator states and seeding-site efficacy.Nature communications · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
How nuclear condensates encode cell-signaling dynamics remains unclear. Photobodies (PBs) in Arabidopsis offer a genetically tractable paradigm. PBs are light- and temperature-sensing nuclear condensates organized by the thermosensitive photoreceptor phytochrome B (phyB). Recent advances have clarified PB composition and illuminated PB formation and function. phyB is the dominant component and provides scaffold-like determinants that recruit selective signaling partners as primary clients (direct phyB binders) and secondary clients (recruited via primaries), spanning transcription/splicing regulators, E3-ligase components, kinases/phosphatases, and chaperones. These clients connect phyB condensates to diverse environmental and hormonal pathways, positioning PBs as a central hub for signaling integration. PB assembly is driven by condensation encoded in phyB's output module and modulated by its photosensory module, coupling assembly/dissolution to photostate and temperature. PBs nucleate nonrandomly at preferred seeding sites, producing spatially distinct classes with different occurrence frequencies and thermosensitivities. PB formation partitions signaling between PBs and the surrounding nucleoplasm, establishing a 2-compartment photosensory system. Within this architecture, dynamic sequestration in PBs tunes nucleoplasmic transcription factor stability and activity to expand signaling dynamic range and extends phyB control into the night by stabilizing active phyB. We propose that PBs function as an autoregulatory rheostat, dialing nucleoplasmic light sensitivity in proportion to incident irradiance and thereby enabling continuous discrimination of light-intensity changes across multiple orders of magnitude. We suggest that this 2-compartment logic illustrates a general role of membraneless organelles in signaling: using dense-phase dynamics to adjust pathway sensitivity and output in the surrounding dilute phase.
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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 OpenQuestion graph.