Gene Research for GO Annotation Review

Target

• Gene symbol: UVR8
• Organism: Arabidopsis thaliana

UniProt Context

=== UNIPROT METADATA ===
UniProt ID: Q9FN03
Entry Name: UVR8_ARATH
Gene Name: UVR8
Locus Tag: At5g63860 {ECO:0000312|Araport:AT5G63860}
Protein Name: Ultraviolet-B receptor UVR8
Organism: Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxonomy ID: 3702
Function: UV-B specific signaling component that acts as a UV-B photoreceptor and plays a key role in establishing UV-protective responses in plants. Upon UV-B irradiation, UVR8 undergoes an immediate switch from homodimer to monomer, accumulates in the nucleus, interacts with the photomorphogenic repressor COP1 and regulates the expression of the transcription factor HY5 by associating with chromatin (through histone H2B binding) in the HY5 promoter region. UVR8 is involved in controlling aspects of leaf growth and morphogenesis in response to UV- B, is required for normal progression of endocycle and has a regulatory role in stomatal differentiation. Is required for plant circadian clock response to photomorphogenic UV-B light, partly through the transcriptional activation of responsive clock genes. Promotes photosynthetic efficiency at elevated levels of UV-B. Plays a role in mediating the effects of UV-B radiation on pathogen resistance by controlling the expression of the sinapate biosynthetic pathway. The two tryptophans, Trp-285 and Trp-233, serve collectively as the UV-B chromophore.
Subcellular Location: Nucleus
Subunit: Homodimer in the absence of UV-B, but absorption of UV-B induces monomerization of UVR8 and interaction with COP1. Interacts with RUP1, RUP2 and histone H2B.
======================

Research Objective

Prepare a comprehensive literature-backed research report for GO annotation review of the target gene.

Focus on:

1. The core biochemical activity of the gene product and any substrate specificity.
2. The activation or maturation mechanism of the protein, including proteolytic processing if relevant.
3. The best-supported subcellular localization and complexes where the active protein functions.
4. The strongest experimentally supported biological processes in the target organism, or in very close orthologs when transfer is justified.
5. Which annotations appear to reflect core function versus context-specific, pleiotropic, or over-extended roles.
6. Any evidence bearing on apoptosis, developmental cell death, neuronal roles, inflammatory signaling, pyroptosis, synaptic remodeling, protein processing, and localization to cytoplasm, cytosol, nucleus, or signaling complexes.

Output Requirements

Structure the report as:

1. Executive summary
2. Molecular function
3. Biological process roles
4. Cellular localization and complexes
5. Annotation-risk assessment
6. Key literature

Use citations for all substantive claims.

Gene Research Report for GO Annotation Review: UVR8 (At5g63860) in Arabidopsis thaliana

1. Executive summary

UVR8 (UV RESISTANCE LOCUS 8) is a UV-B–specific photoreceptor that initiates UV-B signaling via a light-triggered homodimer → monomer photoconversion mediated by intrinsic tryptophan chromophores (especially Trp285 and Trp233) rather than by any enzymatic catalysis or proteolytic maturation. Upon UV-B activation, UVR8 monomers interact with COP1, resulting in transcriptional reprogramming (largely via HY5/HYH) that drives UV-protective acclimation (e.g., phenylpropanoid/flavonoid production) and characteristic photomorphogenic outputs. Strong, recent mechanistic work (2023–2024) refines regulation of the pathway: RUP2-mediated redimerization is explained structurally by two binding interfaces, and UVR8 phosphorylation (S402) modulates partner binding (especially RUP1/2) and flavonoid outcomes. UVR8 is predominantly cytoplasmic in the absence of UV-B but shows rapid UV-B–induced nuclear accumulation (minutes), where signaling is executed. Evidence that UVR8 directly binds chromatin/histones (H2B) is conflicting, with earlier ChIP/histone-binding reports but later rigorous ChIP/nucleosome-binding experiments failing to confirm specific chromatin association.

Critically for GO curation, available evidence does not support annotation of UVR8 with proteolytic activation/processing, apoptosis/pyroptosis-like pathways, neuronal/synaptic roles, or mammalian inflammatory signaling. UV-induced programmed cell death in plants is typically attributed to damage/ROS/MAPK stress pathways, which are conceptually distinct from the UVR8-mediated photomorphogenic/acclimation pathway.

A curated evidence synopsis (with quantitative details) is provided below.

Table: This table summarizes the strongest molecular function, biological process, localization, complex, and regulatory evidence for Arabidopsis UVR8, with emphasis on GO curation confidence and annotation risk. It highlights core functions versus context-specific or disputed claims and includes key quantitative details from foundational and recent studies.

2. Molecular function (GO: Molecular Function)

2.1 Core biochemical activity: UV-B photoreceptor/light sensor (non-enzymatic)

UVR8’s best-supported “molecular function” is photoreception of UV-B radiation. UVR8 lacks an exogenous chromophore; instead, UV-B is absorbed by intrinsic tryptophan residues clustered at the dimer interface. Mutational evidence highlights Trp285 as the principal chromophore residue with Trp233 also essential for correct photoperception/photoconversion, consistent with UVR8 functioning as a UV-B receptor rather than as an enzyme with a substrate-binding pocket. (tilbrook2013theuvr8uvb pages 5-6, yang2015howdoesphotoreceptor pages 3-4)

2.2 Activation mechanism: UV-B–induced dimer dissociation; C-terminal signaling region

Activation is a reversible conformational switch: UV-B perception triggers UVR8 homodimer dissociation into monomers by disrupting an intersubunit salt-bridge network. Constitutive monomer and constitutive dimer mutants (e.g., W285A versus W285F) support that monomerization is the signaling-competent state. (tilbrook2013theuvr8uvb pages 5-6, jenkins2014theuvbphotoreceptor pages 4-5)

A conserved C-terminal 27-aa region (C27) is required for signaling output: C27 deletion mutants can still monomerize and accumulate in the nucleus but show compromised signaling, indicating that photoconversion/nuclear presence is necessary but not sufficient without appropriate protein–protein interaction interfaces. (tilbrook2013theuvr8uvb pages 9-11)

2.3 Binding partners and specificity

COP1 binding: UVR8 monomers interact with COP1 in a UV-B-dependent manner; genetic and interaction data support that COP1 binds the monomeric UVR8 state (consistent with constitutive monomer/dimer UVR8 mutant behaviors). (tilbrook2013theuvr8uvb pages 7-9, tilbrook2013theuvr8uvb pages 9-11)

RUP1/RUP2 binding (negative feedback): RUP proteins bind UVR8 (including UVR8W285A in a UV-B-independent fashion) and facilitate UVR8 return to the homodimeric ground state. A high-resolution structure (2.0 Å) shows RUP2–UVR8 heterodimerization via two interfaces, one involving the C27/VP region and one involving the UVR8 core, explaining accelerated redimerization relative to autonomous recovery. (wang2023rup2facilitatesuvr8 pages 1-3, wang2023rup2facilitatesuvr8 pages 3-6)

Phosphorylation-dependent binding modulation (2024): UVR8 is phosphorylated at multiple sites; Ser402 in C27 is the principal UV-B-stimulated site. A phosphomimetic S402D variant shows strongly increased binding to RUP1/2 (with no consistent COP1 binding change), linking post-translational modification to selective partner engagement and output tuning. Quantitatively, ^32P incorporation into UVR8 rose ~1.5-fold after 24 h UV-B; S402A retained ~28% of WT labeling under UV-B. (liu2024phosphorylationofarabidopsis pages 2-3, liu2024phosphorylationofarabidopsis pages 5-6)

2.4 Proteolytic processing/maturation

Across core UVR8 mechanistic sources, UVR8 activation is repeatedly described as photoconversion (dimer→monomer) without proteolytic cleavage, and no experimentally supported UVR8 cleavage/maturation step is presented. Thus, proteolytic processing should not be annotated as a UVR8 activation mechanism. (jenkins2014theuvbphotoreceptor pages 4-5, tilbrook2013theuvr8uvb pages 6-7)

3. Biological process roles (GO: Biological Process)

3.1 Strongest UVR8-dependent processes (core)

UV-B photomorphogenesis and UV-B signaling: UVR8 mediates canonical low-fluence UV-B photomorphogenic outputs such as hypocotyl growth inhibition and broader developmental photomorphogenesis responses. These are core UVR8 pathway phenotypes and are strengthened by UVR8–COP1 interaction evidence and genetic phenotypes. (jenkins2014theuvbphotoreceptor pages 4-5, tilbrook2013theuvr8uvb pages 13-14)

UV-protective secondary metabolism: UVR8 promotes transcriptional induction of phenylpropanoid/flavonoid pathway genes (e.g., CHS) and accumulation of UV-absorbing/photoprotective metabolites. Transcriptomic analyses report UVR8 regulates >70 genes in mature leaves and several hundred genes in seedlings under UV-B. (jenkins2014theuvbphotoreceptor pages 2-3, morales2013multiplerolesfor pages 1-2)

Transcriptional regulation with chromatin mark changes: UVR8 signaling correlates with UV-B-induced histone acetylation changes at UVR8-responsive loci. A ChIP-seq study identified 133 loci with UV-B-induced, UVR8-dependent H3K9/14 diacetylation, with 39% overlapping previously known UVR8-regulated genes. This supports annotating UVR8 as a regulator of transcriptional responses to UV-B, though it does not alone prove UVR8 is a chromatin-binding protein. (velanis2016regulationoftranscription pages 12-15)

3.2 Context-specific or pleiotropic outputs (supported but higher annotation risk)

UVR8 has documented roles in additional phenotypes/processes including leaf growth and epidermal cell expansion, stomatal index increase, endoreduplication in epidermal cells, and circadian clock entrainment by low-fluence UV-B. These are experimentally supported phenotypic outputs but may reflect downstream transcriptional and hormonal network effects rather than UVR8 “core biochemical function.” (jenkins2014theuvbphotoreceptor pages 4-5, jenkins2014theuvbphotoreceptor pages 2-3)

UVR8-dependent changes also associate with pathogen resistance and other stress interactions under solar UV (e.g., reduced UV-B–enhanced resistance to Botrytis cinerea in uvr8 mutants). These are biologically meaningful but are best treated as downstream consequences of UV-B acclimation programs, not as defining UVR8 molecular function. (jenkins2014theuvbphotoreceptor pages 3-4)

3.3 Distinguishing UVR8 signaling from UV-B damage/PCD responses

Plant UV-induced programmed cell death is commonly attributed to stress/damage pathways (e.g., ROS and MAPK cascades) distinct from UVR8 photomorphogenesis. A UV-induced cell-death review explicitly separates the UVR8-regulated photomorphogenic pathway from UV-B stress/MAPK pathways implicated in PCD and describes the role of UVR8 under stress as unclear/“obscure,” providing no direct UVR8→PCD mechanism. (nawkar2013uvinducedcelldeath pages 6-8, nawkar2013uvinducedcelldeath pages 1-3)

4. Cellular localization and complexes (GO: Cellular Component / Complex)

4.1 Subcellular localization

UVR8 is present in both cytoplasmic and nuclear pools, with the majority cytoplasmic before UV-B and a smaller nuclear pool. UV-B rapidly increases nuclear accumulation: microscopy/fusion-protein studies report nuclear localization detectable in ~5 minutes, with ~90% of nuclei showing signal after UV-B. Total UVR8 protein abundance does not change substantially during this relocalization. (jenkins2014theuvbphotoreceptor pages 8-9, tilbrook2013theuvr8uvb pages 6-7)

UVR8 lacks an obvious canonical NLS, but the N-terminal 23 amino acids are required for UV-B-induced nuclear accumulation. Notably, nuclear localization alone is insufficient to activate signaling; UV-B/monomerization remains required. (tilbrook2013theuvr8uvb pages 6-7)

4.2 Complexes and regulatory modules

UVR8–COP1 complex: UV-B triggers UVR8–COP1 interaction; COP1 accumulates in the nucleus upon UV-B, consistent with nuclear execution of UVR8 signaling. (tilbrook2013theuvr8uvb pages 7-9, jenkins2014theuvbphotoreceptor pages 8-9)

UVR8–RUP module: RUP1/2 accelerate UVR8 redimerization and terminate signaling. Genetic evidence indicates RUP-mediated redimerization occurs independently of COP1, consistent with a negative-feedback module that resets UVR8’s ground state. (heijde2013reversionofthe pages 4-5)

RUP2 two-interface model (visual evidence): Structural data depict the RUP2–UVR8 complex and two interfaces supporting redimerization acceleration; these panels are important for curator interpretation of the molecular mechanism of negative feedback. (wang2023rup2facilitatesuvr8 media cc99b673, wang2023rup2facilitatesuvr8 media 33c4c55d)

4.3 Chromatin/histone association (controversial)

Earlier studies (summarized in major reviews) reported UVR8 recovery in chromatin preparations, ChIP recovery at promoters of UVR8-regulated genes, and preferential binding to histone H2B in histone-agarose assays, suggesting chromatin association. (jenkins2014theuvbphotoreceptor pages 10-11, tilbrook2013theuvr8uvb pages 6-7)

However, a careful re-examination using controlled ChIP-qPCR (endogenous UVR8 and tagged UVR8), matched crosslinked chromatin pools, and in vitro nucleosome-binding assays did not detect UVR8 association at HY5/MYB12 loci and found recombinant UVR8 does not bind nucleosomes, arguing against a core “chromatin binding” function. Thus, direct chromatin-binding annotations should be treated as high risk or qualified. (binkert2016revisitingchromatinbinding pages 2-4, binkert2016revisitingchromatinbinding pages 1-2)

5. Annotation-risk assessment (GO curation guidance)

5.1 Likely core/robust annotations (high confidence)

1. UV-B photoreceptor / UV-B sensing via intrinsic tryptophans and photoconversion (dimer→monomer). (tilbrook2013theuvr8uvb pages 5-6, jenkins2014theuvbphotoreceptor pages 4-5)
2. Protein binding to COP1 upon UV-B activation; UVR8–COP1 complex as central signaling node. (tilbrook2013theuvr8uvb pages 7-9, tilbrook2013theuvr8uvb pages 9-11)
3. Negative feedback regulation of UVR8 signaling via RUP1/RUP2-mediated redimerization (including mechanistic structural support). (heijde2013reversionofthe pages 4-5, wang2023rup2facilitatesuvr8 pages 3-6)
4. UV-B–induced nuclear accumulation / nuclear signaling role, with explicit UV-B-dependent kinetics. (jenkins2014theuvbphotoreceptor pages 8-9, tilbrook2013theuvr8uvb pages 6-7)
5. Regulation of UV-protective phenylpropanoid/flavonoid biosynthesis and broader UV-B transcriptional acclimation. (jenkins2014theuvbphotoreceptor pages 2-3, morales2013multiplerolesfor pages 1-2)

5.2 Medium-confidence or context-specific annotations (use with care)

1. Circadian clock entrainment by photomorphogenic UV-B: experimentally supported but may be annotated more conservatively as regulation of circadian rhythm under UV-B. (jenkins2014theuvbphotoreceptor pages 4-5)
2. Stomatal development and endoreduplication: supported phenotypically but mechanisms are less direct; these may reflect downstream growth regulation and could be over-extended if treated as direct UVR8 biochemical functions. (jenkins2014theuvbphotoreceptor pages 4-5)
3. Pathogen resistance outcomes: best interpreted as downstream of UV-protective metabolic and transcriptional programs. (jenkins2014theuvbphotoreceptor pages 3-4)

5.3 High-risk / disputed / not supported annotations

1. Direct chromatin binding / histone H2B binding as a core UVR8 activity is disputed; later data challenge locus-specific ChIP and nucleosome binding. If included, it should be carefully evidence-coded and perhaps qualified as controversial. (jenkins2014theuvbphotoreceptor pages 10-11, binkert2016revisitingchromatinbinding pages 1-2)
2. Proteolytic processing / cleavage activation of UVR8: not supported; activation is photoconversion. (jenkins2014theuvbphotoreceptor pages 4-5, tilbrook2013theuvr8uvb pages 6-7)
3. Apoptosis, pyroptosis, inflammatory signaling, neuronal/synaptic roles: no relevant experimental evidence for Arabidopsis UVR8; UV-induced PCD literature largely attributes cell death to UV damage/ROS/MAPK pathways, not UVR8 signaling. (nawkar2013uvinducedcelldeath pages 6-8, nawkar2013uvinducedcelldeath pages 1-3)

6. Key literature (prioritized; includes URLs and dates)

Recent primary (2023–2024):
- Liu W. et al. Nature Communications (Feb 2024). “Phosphorylation of Arabidopsis UVR8 photoreceptor modulates protein interactions and responses to UV-B radiation.” https://doi.org/10.1038/s41467-024-45575-7 (liu2024phosphorylationofarabidopsis pages 2-3, liu2024phosphorylationofarabidopsis pages 5-6)
- Wang L. et al. Plant Communications (Jan 2023). “RUP2 facilitates UVR8 redimerization via two interfaces.” https://doi.org/10.1016/j.xplc.2022.100428 (wang2023rup2facilitatesuvr8 pages 1-3, wang2023rup2facilitatesuvr8 pages 3-6)

Foundational reviews / synthesis:
- Jenkins GI. The Plant Cell (Jan 2014). “The UV-B Photoreceptor UVR8: From Structure to Physiology.” https://doi.org/10.1105/tpc.113.119446 (jenkins2014theuvbphotoreceptor pages 4-5, jenkins2014theuvbphotoreceptor pages 2-3)
- Tilbrook K. et al. The Arabidopsis Book (Jun 2013). “The UVR8 UV-B Photoreceptor: Perception, Signaling and Response.” https://doi.org/10.1199/tab.0164 (tilbrook2013theuvr8uvb pages 6-7, tilbrook2013theuvr8uvb pages 9-11)

Chromatin association dispute:
- Binkert M. et al. BMC Plant Biology (Feb 2016). “Revisiting chromatin binding of the Arabidopsis UV-B photoreceptor UVR8.” https://doi.org/10.1186/s12870-016-0732-5 (binkert2016revisitingchromatinbinding pages 2-4, binkert2016revisitingchromatinbinding pages 1-2)
- Velanis CN. et al. Plant Molecular Biology (Aug 2016). “Regulation of transcription by the Arabidopsis UVR8 photoreceptor involves a specific histone modification.” https://doi.org/10.1007/s11103-016-0522-3 (velanis2016regulationoftranscription pages 12-15)

UVR8 vs UV-induced cell death context:
- Nawkar GM. et al. International Journal of Molecular Sciences (Jan 2013). “UV-Induced Cell Death in Plants.” https://doi.org/10.3390/ijms14011608 (nawkar2013uvinducedcelldeath pages 6-8, nawkar2013uvinducedcelldeath pages 1-3)

Notes on “current applications and real-world implementations”

In applied settings, UVR8 is widely treated as a molecular handle to engineer UV-B responses and UV-protective metabolite production (e.g., enhancing phenylpropanoid/flavonoid accumulation) and as a model photoswitch in heterologous contexts; however, within the provided evidence corpus here, the strongest directly citable recent “implementation-level” evidence pertains to mechanistic control of flavonoid biosynthesis via UVR8 phosphorylation (S402) and negative-feedback resetting via RUP2 structure/function, which could inform crop or synthetic biology strategies. (liu2024phosphorylationofarabidopsis pages 5-6, wang2023rup2facilitatesuvr8 pages 3-6)

References

1. (tilbrook2013theuvr8uvb pages 5-6): Kimberley Tilbrook, Adriana B. Arongaus, Melanie Binkert, Marc Heijde, Ruohe Yin, and Roman Ulm. The uvr8 uv-b photoreceptor: perception, signaling and response. The Arabidopsis Book, 2013:e0164, Jun 2013. URL: https://doi.org/10.1199/tab.0164, doi:10.1199/tab.0164. This article has 362 citations and is from a peer-reviewed journal.

2. (yang2015howdoesphotoreceptor pages 3-4): Xiaojing Yang, Sherwin Montano, and Zhong Ren. How does photoreceptor uvr8 perceive a uv‐b signal? Photochemistry and Photobiology, 91:993-1003, Sep 2015. URL: https://doi.org/10.1111/php.12470, doi:10.1111/php.12470. This article has 32 citations and is from a peer-reviewed journal.

3. (jenkins2014theuvbphotoreceptor pages 4-5): Gareth I. Jenkins. The uv-b photoreceptor uvr8: from structure to physiology. Plant Cell, 26:21-37, Jan 2014. URL: https://doi.org/10.1105/tpc.113.119446, doi:10.1105/tpc.113.119446. This article has 463 citations and is from a highest quality peer-reviewed journal.

4. (tilbrook2013theuvr8uvb pages 7-9): Kimberley Tilbrook, Adriana B. Arongaus, Melanie Binkert, Marc Heijde, Ruohe Yin, and Roman Ulm. The uvr8 uv-b photoreceptor: perception, signaling and response. The Arabidopsis Book, 2013:e0164, Jun 2013. URL: https://doi.org/10.1199/tab.0164, doi:10.1199/tab.0164. This article has 362 citations and is from a peer-reviewed journal.

5. (tilbrook2013theuvr8uvb pages 9-11): Kimberley Tilbrook, Adriana B. Arongaus, Melanie Binkert, Marc Heijde, Ruohe Yin, and Roman Ulm. The uvr8 uv-b photoreceptor: perception, signaling and response. The Arabidopsis Book, 2013:e0164, Jun 2013. URL: https://doi.org/10.1199/tab.0164, doi:10.1199/tab.0164. This article has 362 citations and is from a peer-reviewed journal.

6. (wang2023rup2facilitatesuvr8 pages 3-6): Lixia Wang, Yidong Wang, Hongfei Chang, Hui Ren, Xinquan Wu, Jia Wen, Zeyuan Guan, Ling Ma, Liang Qiu, Junjie Yan, Delin Zhang, Xi Huang, and Ping Yin. Rup2 facilitates uvr8 redimerization via two interfaces. Jan 2023. URL: https://doi.org/10.1016/j.xplc.2022.100428, doi:10.1016/j.xplc.2022.100428. This article has 23 citations and is from a peer-reviewed journal.

7. (heijde2013reversionofthe pages 4-5): Marc Heijde and Roman Ulm. Reversion of the arabidopsis uv-b photoreceptor uvr8 to the homodimeric ground state. Proceedings of the National Academy of Sciences, 110:1113-1118, Dec 2013. URL: https://doi.org/10.1073/pnas.1214237110, doi:10.1073/pnas.1214237110. This article has 261 citations and is from a highest quality peer-reviewed journal.

8. (wang2023rup2facilitatesuvr8 pages 1-3): Lixia Wang, Yidong Wang, Hongfei Chang, Hui Ren, Xinquan Wu, Jia Wen, Zeyuan Guan, Ling Ma, Liang Qiu, Junjie Yan, Delin Zhang, Xi Huang, and Ping Yin. Rup2 facilitates uvr8 redimerization via two interfaces. Jan 2023. URL: https://doi.org/10.1016/j.xplc.2022.100428, doi:10.1016/j.xplc.2022.100428. This article has 23 citations and is from a peer-reviewed journal.

9. (wang2023rup2facilitatesuvr8 media cc99b673): Lixia Wang, Yidong Wang, Hongfei Chang, Hui Ren, Xinquan Wu, Jia Wen, Zeyuan Guan, Ling Ma, Liang Qiu, Junjie Yan, Delin Zhang, Xi Huang, and Ping Yin. Rup2 facilitates uvr8 redimerization via two interfaces. Jan 2023. URL: https://doi.org/10.1016/j.xplc.2022.100428, doi:10.1016/j.xplc.2022.100428. This article has 23 citations and is from a peer-reviewed journal.

10. (tilbrook2013theuvr8uvb pages 6-7): Kimberley Tilbrook, Adriana B. Arongaus, Melanie Binkert, Marc Heijde, Ruohe Yin, and Roman Ulm. The uvr8 uv-b photoreceptor: perception, signaling and response. The Arabidopsis Book, 2013:e0164, Jun 2013. URL: https://doi.org/10.1199/tab.0164, doi:10.1199/tab.0164. This article has 362 citations and is from a peer-reviewed journal.

11. (jenkins2014theuvbphotoreceptor pages 8-9): Gareth I. Jenkins. The uv-b photoreceptor uvr8: from structure to physiology. Plant Cell, 26:21-37, Jan 2014. URL: https://doi.org/10.1105/tpc.113.119446, doi:10.1105/tpc.113.119446. This article has 463 citations and is from a highest quality peer-reviewed journal.

12. (tilbrook2013theuvr8uvb pages 13-14): Kimberley Tilbrook, Adriana B. Arongaus, Melanie Binkert, Marc Heijde, Ruohe Yin, and Roman Ulm. The uvr8 uv-b photoreceptor: perception, signaling and response. The Arabidopsis Book, 2013:e0164, Jun 2013. URL: https://doi.org/10.1199/tab.0164, doi:10.1199/tab.0164. This article has 362 citations and is from a peer-reviewed journal.

13. (jenkins2014theuvbphotoreceptor pages 2-3): Gareth I. Jenkins. The uv-b photoreceptor uvr8: from structure to physiology. Plant Cell, 26:21-37, Jan 2014. URL: https://doi.org/10.1105/tpc.113.119446, doi:10.1105/tpc.113.119446. This article has 463 citations and is from a highest quality peer-reviewed journal.

14. (morales2013multiplerolesfor pages 1-2): Luis O. Morales, Mikael Brosché, Julia Vainonen, Gareth I. Jenkins, Jason J. Wargent, Nina Sipari, Åke Strid, Anders V. Lindfors, Riitta Tegelberg, and Pedro J. Aphalo. Multiple roles for uv resistance locus8 in regulating gene expression and metabolite accumulation in arabidopsis under solar ultraviolet radiation. Plant Physiology, 161:744-759, Dec 2013. URL: https://doi.org/10.1104/pp.112.211375, doi:10.1104/pp.112.211375. This article has 242 citations and is from a highest quality peer-reviewed journal.

15. (liu2024phosphorylationofarabidopsis pages 1-2): Wei Liu, Giovanni Giuriani, Anezka Havlikova, Dezhi Li, Douglas J. Lamont, Susanne Neugart, Christos N. Velanis, Jan Petersen, Ute Hoecker, John M. Christie, and Gareth I. Jenkins. Phosphorylation of arabidopsis uvr8 photoreceptor modulates protein interactions and responses to uv-b radiation. Nature Communications, Feb 2024. URL: https://doi.org/10.1038/s41467-024-45575-7, doi:10.1038/s41467-024-45575-7. This article has 33 citations and is from a highest quality peer-reviewed journal.

16. (liu2024phosphorylationofarabidopsis pages 2-3): Wei Liu, Giovanni Giuriani, Anezka Havlikova, Dezhi Li, Douglas J. Lamont, Susanne Neugart, Christos N. Velanis, Jan Petersen, Ute Hoecker, John M. Christie, and Gareth I. Jenkins. Phosphorylation of arabidopsis uvr8 photoreceptor modulates protein interactions and responses to uv-b radiation. Nature Communications, Feb 2024. URL: https://doi.org/10.1038/s41467-024-45575-7, doi:10.1038/s41467-024-45575-7. This article has 33 citations and is from a highest quality peer-reviewed journal.

17. (liu2024phosphorylationofarabidopsis pages 5-6): Wei Liu, Giovanni Giuriani, Anezka Havlikova, Dezhi Li, Douglas J. Lamont, Susanne Neugart, Christos N. Velanis, Jan Petersen, Ute Hoecker, John M. Christie, and Gareth I. Jenkins. Phosphorylation of arabidopsis uvr8 photoreceptor modulates protein interactions and responses to uv-b radiation. Nature Communications, Feb 2024. URL: https://doi.org/10.1038/s41467-024-45575-7, doi:10.1038/s41467-024-45575-7. This article has 33 citations and is from a highest quality peer-reviewed journal.

18. (velanis2016regulationoftranscription pages 12-15): Christos N. Velanis, Pawel Herzyk, and Gareth I. Jenkins. Regulation of transcription by the arabidopsis uvr8 photoreceptor involves a specific histone modification. Plant Molecular Biology, 92:425-443, Aug 2016. URL: https://doi.org/10.1007/s11103-016-0522-3, doi:10.1007/s11103-016-0522-3. This article has 40 citations and is from a peer-reviewed journal.

19. (jenkins2014theuvbphotoreceptor pages 10-11): Gareth I. Jenkins. The uv-b photoreceptor uvr8: from structure to physiology. Plant Cell, 26:21-37, Jan 2014. URL: https://doi.org/10.1105/tpc.113.119446, doi:10.1105/tpc.113.119446. This article has 463 citations and is from a highest quality peer-reviewed journal.

20. (binkert2016revisitingchromatinbinding pages 1-2): Melanie Binkert, Carlos D. Crocco, Babatunde Ekundayo, Kelvin Lau, Sarah Raffelberg, Kimberley Tilbrook, Ruohe Yin, Richard Chappuis, Thomas Schalch, and Roman Ulm. Revisiting chromatin binding of the arabidopsis uv-b photoreceptor uvr8. BMC Plant Biology, Feb 2016. URL: https://doi.org/10.1186/s12870-016-0732-5, doi:10.1186/s12870-016-0732-5. This article has 45 citations and is from a peer-reviewed journal.

21. (binkert2016revisitingchromatinbinding pages 2-4): Melanie Binkert, Carlos D. Crocco, Babatunde Ekundayo, Kelvin Lau, Sarah Raffelberg, Kimberley Tilbrook, Ruohe Yin, Richard Chappuis, Thomas Schalch, and Roman Ulm. Revisiting chromatin binding of the arabidopsis uv-b photoreceptor uvr8. BMC Plant Biology, Feb 2016. URL: https://doi.org/10.1186/s12870-016-0732-5, doi:10.1186/s12870-016-0732-5. This article has 45 citations and is from a peer-reviewed journal.

22. (binkert2016revisitingchromatinbinding pages 4-5): Melanie Binkert, Carlos D. Crocco, Babatunde Ekundayo, Kelvin Lau, Sarah Raffelberg, Kimberley Tilbrook, Ruohe Yin, Richard Chappuis, Thomas Schalch, and Roman Ulm. Revisiting chromatin binding of the arabidopsis uv-b photoreceptor uvr8. BMC Plant Biology, Feb 2016. URL: https://doi.org/10.1186/s12870-016-0732-5, doi:10.1186/s12870-016-0732-5. This article has 45 citations and is from a peer-reviewed journal.

23. (jenkins2014theuvbphotoreceptor pages 3-4): Gareth I. Jenkins. The uv-b photoreceptor uvr8: from structure to physiology. Plant Cell, 26:21-37, Jan 2014. URL: https://doi.org/10.1105/tpc.113.119446, doi:10.1105/tpc.113.119446. This article has 463 citations and is from a highest quality peer-reviewed journal.

24. (nawkar2013uvinducedcelldeath pages 6-8): Ganesh M. Nawkar, Punyakishore Maibam, Jung Hoon Park, V. Sahi, Sang Yeol Lee, and Chang Ho Kang. Uv-induced cell death in plants. International Journal of Molecular Sciences, 14:1608-1628, Jan 2013. URL: https://doi.org/10.3390/ijms14011608, doi:10.3390/ijms14011608. This article has 341 citations.

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