ReviewJournal of experimental botany2025
Recent advances in UV-B signalling: interaction of proteins with the UVR8 photoreceptor.
Review in Journal of experimental botany, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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
6 citing papers in PubMed, 14 citations in OpenAlex.
- Phosphorylation of the plant photoreceptor UVR8 regulates its dimer/monomer status and enhances UV-B signaling across species.The Plant cell · 2026Article
- UVR8-mediated UV-B signaling and its regulation of horticultural traits: from Arabidopsis to application.Horticulture research · 2026Review
- Transcription factors interact with Arabidopsis UVR8 photoreceptor at distinct sites to COP1 and RUP proteins.The Plant journal : for cell and molecular biology · 2026Article
- Epigenetic regulation under light and temperature fluctuations: chromatin remodeling and transcriptional memory in plants.Plant cell reports · 2026Review
- Learning from nature: phytochemical strategies to protect against UV-B damage.Nature communications · 2025Review
- Flavonoid pathway intermediates implicate UVR8 in functions beyond canonical UV-B signaling.Nature communications · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
The UV RESISTANCE LOCUS 8 (UVR8) photoreceptor mediates many plant responses to UV-B and short wavelength UV-A light. UVR8 functions through interactions with other proteins which lead to extensive changes in gene expression. Interactions with particular proteins determine the nature of the response to UV-B. It is therefore important to understand the molecular basis of these interactions: how are different proteins able to bind to UVR8 and how is differential binding regulated? This concise review highlights recent developments in addressing these questions. Key advances are discussed with regard to: identification of proteins that interact with UVR8; the mechanism of UVR8 accumulation in the nucleus; the photoactivation of UVR8 monomer; the structural basis of interaction between UVR8 and CONSTITUTIVELY PHOTOMORPHOGENIC 1 (COP1) and REPRESSOR OF UV-B PHOTOMORPHOGENESIS (RUP) proteins; and the role of UVR8 phosphorylation in modulating interactions and responses to UV-B. Nevertheless, much remains to be understood, and the need to extend future research to the growing list of interactors is emphasized.
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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.