Gene Research for GO Annotation Review

Target

• Gene symbol: ZTL
• Organism: Arabidopsis thaliana

UniProt Context

=== UNIPROT METADATA ===
UniProt ID: F4KAN2
Entry Name: F4KAN2_ARATH
Gene Name: ZTL
Locus Tag: At5g57360 {ECO:0000313|Araport:AT5G57360,
Gene Synonyms: ADAGIO 1 {ECO:0000313|EMBL:AED96892.1}, ADO1
Organism: Arabidopsis thaliana (Mouse-ear cress)
NCBI Taxonomy ID: 3702 {ECO:0000313|EMBL:AED96892.1, ECO:0000313|Proteomes:UP000006548}
Subcellular Location: Nucleus
======================

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: ZEITLUPE (ZTL/ADO1) in Arabidopsis thaliana (At5g57360; UniProt F4KAN2)

1. Executive summary

ZEITLUPE (ZTL; also known historically as ADAGIO1/ADO1) encodes a plant-specific blue-light-sensing F-box protein with a canonical LOV–F-box–Kelch repeat domain architecture. The best-supported core biochemical role of ZTL is as the substrate recognition component of an SCF-type E3 ubiquitin ligase (SCF^ZTL) that drives 26S proteasome-dependent degradation of specific circadian clock proteins, particularly TOC1 (PRR1) and PRR5, thereby setting circadian period and oscillator robustness. Substrate recruitment is light- and phosphorylation-dependent (blue light stabilizes ZTL and inhibits turnover; hyperphosphorylated PRR5/TOC1 bind ZTL better), consistent with ZTL acting as a photoreceptor-coupled proteostasis regulator in the oscillator. (kiba2007targeteddegradationof pages 1-3, kiba2007targeteddegradationof pages 8-9, fujiwara2008posttranslationalregulationof pages 6-6, fujiwara2008posttranslationalregulationof pages 1-2)

Recent work extends ZTL’s influence beyond canonical clock components by implicating ZTL in proteasome-linked diel regulation of growth signaling proteins (e.g., persistent phosphorylated S6K in ztl-3), suggesting ZTL can couple clock/photoperiod information to TOR-dependent translational capacity. (boix202440sribosomalprotein pages 3-4, boix202440sribosomalprotein pages 8-9)

On cellular component/localization, the strongest direct evidence supports cytosol-enriched ZTL (and ZTL-LOV) and a key mechanistic function in modulating nucleocytoplasmic partitioning of GIGANTEA (GI) through LOV-dependent binding and sequestration; ZTL thereby indirectly impacts flowering-time networks that depend on GI nuclear functions. (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 5-7, kim2013thefboxprotein media fe7aa0b6)

Quantitatively, a 2024 Science Advances study provides strong, recent genetic evidence that ZTL is a major determinant of circadian period across temperatures, with ztl mutants exhibiting periods ~1.7–3.6 h longer than wild type depending on temperature regime, and explicitly links ZTL/LKP2-mediated clock protein degradation to temperature compensation. (maeda2024coldinduceddegradationof pages 7-8)

No evidence in the curated plant literature supports ZTL roles in apoptosis, pyroptosis, neuronal/synaptic biology, or inflammatory signaling (animal-specific processes); any such annotations would represent cross-kingdom over-extension. (fu2025apathogeneffector pages 6-7, kiba2007targeteddegradationof pages 1-3)

2. Molecular function

2.1 Core biochemical activity: SCF E3 ligase substrate adaptor (F-box protein)

Definition (GO-relevant concept): An F-box protein typically functions as a substrate adaptor in an SCF (Skp1–Cullin–F-box–Rbx1) ubiquitin ligase, recruiting specific substrates for polyubiquitination and subsequent 26S proteasome degradation.

ZTL’s best-supported molecular function: ZTL functions as a blue-light-regulated F-box substrate adaptor in an SCF E3 ligase that controls proteasome-mediated turnover of circadian proteins. (kiba2007targeteddegradationof pages 1-3, harmon2008cul1regulatestoc1 pages 1-2, suetsugu2013evolutionofthree pages 7-8)

Key experimental support includes:
- PRR5 targeting: PRR5 binds ZTL in vivo and in vitro in a PR-domain-dependent manner, and PRR5 half-life is shorter in dark conditions; the authors explicitly propose ZTL targets PRR5 for 26S proteasome degradation. (kiba2007targeteddegradationof pages 1-3, kiba2007targeteddegradationof pages 8-9)
- TOC1 targeting and SCF dependence: CUL1 function is required for TOC1 stability control, and reduced CUL1 activity phenocopies ztl long-period phenotypes, supporting TOC1 turnover as SCF-dependent with ZTL as F-box adaptor. (harmon2008cul1regulatestoc1 pages 1-2)
- SCF complex membership evidence: Experimental literature summarized in comparative analyses indicates ZTL co-immunoprecipitates with core SCF components (ASK1/CUL1/AtRBX1) and that SCF component perturbations phenocopy ztl circadian phenotypes. (suetsugu2013evolutionofthree pages 7-8)

2.2 Substrate specificity and experimentally supported interactors

Canonical clock substrates (strongest support):
- PRR5: Physical interaction (co-IP), interaction domain dependence (PR domain), and genetic dependence of ztl phenotypes on PRR5 support PRR5 as a direct ZTL substrate. (kiba2007targeteddegradationof pages 8-9, kiba2007targeteddegradationof pages 11-12, kiba2007targeteddegradationof pages 1-3)
- TOC1 (PRR1): Established as an SCF^ZTL proteolysis target; ZTL/TOC1 interaction and SCF dependency is supported by CUL1 genetic evidence and by biochemical context in clock proteolysis studies. (harmon2008cul1regulatestoc1 pages 1-2, fujiwara2008posttranslationalregulationof pages 1-2)

Non-substrate binding partners with strong mechanistic relevance:
- GIGANTEA (GI): ZTL binds GI via the LOV domain; ZTL or ZTL-LOV expression increases GI protein levels post-transcriptionally (~2–4×) and changes GI nucleocytoplasmic distribution. This is best interpreted as ZTL forming a functional complex with GI that impacts GI localization/stability. (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 7-8, kim2013thefboxprotein pages 5-7)

Emerging/newer interactors:
- CHE (CCA1 HIKING EXPEDITION): A 2025 Nature Communications study provides multiple orthogonal assays showing ZTL binds CHE (pull-down, Y2H mapping, BiFC, MST; Kd ~90–386 nM), and shows a pathogen effector can disrupt this interaction to stabilize CHE (consistent with ZTL-mediated degradation). This strongly supports physical interaction; the extent to which CHE should be treated as a core ZTL substrate for GO requires careful consideration because the most direct link to ubiquitination/degradation is mechanistic inference rather than shown ubiquitination in the excerpted evidence. (fu2025apathogeneffector pages 6-7)

Non-canonical growth/proteostasis target (2024):
- S6K (S6 kinase): In a 2024 Plant Physiology study, phosphorylated S6K levels showed abnormal persistence in ztl-3 mutants, and the authors propose proteasome-dependent degradation shaping diel S6K dynamics. This is experimental genetic evidence that ZTL affects S6K phosphorylation/abundance patterns, but direct ZTL→S6K ubiquitination and binding evidence is not yet established in the excerpted text, making this a higher-risk MF extension than TOC1/PRR5. (boix202440sribosomalprotein pages 3-4, boix202440sribosomalprotein pages 8-9)

2.3 Activation/maturation and regulatory mechanisms

Light regulation via LOV domain (blue light photoreception):
- ZTL contains an N-terminal LOV domain (flavin-binding) that functions as a blue-light-regulated switch; blue light inhibits in vivo degradation of ZTL and PRR5 and stabilizes these proteins, consistent with blue-light control of SCF^ZTL activity or substrate engagement. (fujiwara2008posttranslationalregulationof pages 1-2, fujiwara2008novelbluelight pages 1-2)

Phosphorylation-dependent substrate recognition:
- Hyperphosphorylated forms of PRR5 and TOC1 interact most strongly with ZTL, supporting a model where phosphorylation state modulates ZTL-mediated recruitment for proteolysis. (fujiwara2008posttranslationalregulationof pages 1-2)

GI-dependent post-translational stabilization and complex dynamics:
- ZTL and GI reciprocally affect each other’s stability and localization: ZTL or ZTL-LOV increases GI protein without changing GI mRNA, and ZTL’s LOV domain is required for GI binding and partitioning effects. (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 7-8)

Chaperone-assisted maturation (annotation caution):
- A 2024 review of GI notes HSP90 involvement in facilitating maturation of ZTL into an SCF^ZTL ligase complex, but this specific chaperone step is review-summarized in the evidence gathered here rather than directly demonstrated in the extracted primary results. (liu2024giganteaunveiledexploring pages 7-8)

3. Biological process roles

3.1 Circadian rhythm / circadian period control (core biological process)

ZTL is a central post-translational regulator of the Arabidopsis circadian oscillator, acting primarily through protein turnover of TOC1 and PRR5.

Strongest recent quantitative evidence (2024):
- In Science Advances (Sep 2024), ztl mutants show a long circadian period across temperatures, reported as ~1.7–3.6 h longer than wild type depending on temperature conditions. The study provides explicit period measurements at low temperatures (e.g., at 15°C average period for ztl ≈ 27.1 h vs lkp2 ≈ 25.7 h; at 12°C, lkp2 ztl ≈ 30.6 h) and integrates ZTL/LKP2-dependent turnover of TOC1/PRR5 into temperature compensation models. (maeda2024coldinduceddegradationof pages 7-8)

Redundancy and oscillator robustness:
- ZTL works partially redundantly with FKF1 and LKP2; higher-order mutants (e.g., ztl fkf1 and ztl fkf1 lkp2) show increased stabilization of TOC1/PRR5 and more severe clock defects, supporting a shared function in turnover of evening factors and period determination. (baudry2010fboxproteinsfkf1 pages 1-2)

3.2 Photomorphogenesis / red-light seedling responses

ZTL impacts photomorphogenic responses through PRR5 turnover:
- PRR5 shows light-dependent half-life changes and ZTL-dependent instability; genetically, prr5-1 partially suppresses ztl red-light hypersensitivity, linking the ZTL→PRR5 degradation module to red-light seedling phenotypes. (kiba2007targeteddegradationof pages 8-9, kiba2007targeteddegradationof pages 11-12)

This supports GO BP terms connected to photomorphogenesis or seedling de-etiolation responses, but with the mechanistic note that ZTL’s direct action is still ubiquitin-mediated proteolysis of clock/PRR proteins. (kiba2007targeteddegradationof pages 8-9)

3.3 Photoperiodic flowering-time regulation (indirect, network-mediated)

ZTL’s strongest support in flowering regulation is as a component of the GI/FKF1/CO regulatory system, largely through controlling stability/partitioning of GI and influencing CO stability indirectly.

• ZTL interacts with GI and FKF1 and is implicated in CONSTANS (CO) protein stability; a ztl mutant CO protein profile resembles that in gi, and GI stabilizes ZTL and FKF1 proteins. (song2014distinctrolesof pages 1-2)
• ZTL influences GI nuclear vs cytosolic pools; increased nuclear GI can enhance GI–FKF1 complex formation, providing a mechanistic route to flowering-time effects. (kim2013thefboxprotein pages 5-7, kim2013thefboxprotein pages 7-8)

These data support ZTL annotations in regulation of photoperiodism/flowering time but argue that such BP annotations should be framed as regulatory (not “required for flowering”) and tied to clock/photoperiod protein stability control rather than direct transcriptional activation. (kim2013thefboxprotein pages 5-7, song2014distinctrolesof pages 1-2)

3.4 Temperature compensation / temperature-related clock regulation

The 2024 Science Advances study positions ZTL (with LKP2) as a major contributor to maintaining circadian period across temperature variation through temperature-dependent degradation of TOC1/PRR5. (maeda2024coldinduceddegradationof pages 7-8)

This supports BP annotations such as temperature compensation of circadian clock or regulation of circadian rhythm by temperature, with strong recent quantitative genetic evidence. (maeda2024coldinduceddegradationof pages 7-8)

3.5 Emerging applications: clock–growth coupling via TOR/S6K

A 2024 Plant Physiology study connects ZTL to diel S6K regulation, proposing that ZTL affects proteasome-dependent degradation shaping S6K dynamics and thus contributing to daylength-dependent growth regulation. Experimentally, phosphorylated S6K levels are altered in ztl-3, consistent with ZTL-dependent proteostasis effects on a growth regulator. (boix202440sribosomalprotein pages 3-4, boix202440sribosomalprotein pages 8-9)

This line of evidence supports considering (with caution) BP annotations related to regulation of growth in response to photoperiod or proteasome-mediated protein catabolism in the context of metabolic integration; however, the direct biochemical step “ZTL ubiquitinates S6K” is not yet established in the excerpted evidence. (boix202440sribosomalprotein pages 3-4)

3.6 Immunity/stress intersections (annotation caution)

A 2025 Nature Communications paper shows a pathogen effector can disrupt ZTL–CHE binding, stabilizing CHE and perturbing development/immunity programs. This supports an intersection between clock protein turnover and immunity but does not justify animal-style inflammatory signaling annotations. (fu2025apathogeneffector pages 6-7)

4. Cellular localization and complexes

4.1 Best-supported localization

Although UniProt metadata often lists nuclear localization, the strongest direct evidence in the curated primary dataset supports cytosol-enriched ZTL:
- In Kim et al. 2013, GFP-tagged ZTL and ZTL-LOV show cytosol-enriched fluorescence, and ZTL influences the cytosol vs nucleus distribution of GI (increasing cytosolic GI and reducing nuclear GI). (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 5-7)

Primary image evidence for the ZTL-dependent shift in GI partitioning is present in the extracted figure regions showing fractionation and microscopy data (Figures 4–5). (kim2013thefboxprotein media fe7aa0b6, kim2013thefboxprotein media 1c2acaaa)

4.2 Complex membership

SCF^ZTL complex:
- ZTL acts as the substrate adaptor of an SCF-type complex that includes Skp1-like ASK proteins, CUL1, and RBX1, with functional dependence supported by CUL1 mutant phenocopy of ztl circadian defects. (harmon2008cul1regulatestoc1 pages 1-2, suetsugu2013evolutionofthree pages 7-8)

GI–ZTL complex (LOV-mediated):
- ZTL binds GI through its LOV domain; this interaction stabilizes GI post-transcriptionally and regulates GI partitioning, consistent with a functional cytosolic complex important for clock/photoperiod outputs. (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 5-7)

ZTL-family network:
- ZTL acts with its paralogs FKF1 and LKP2 in overlapping control of clock protein stability; genetic evidence supports partial redundancy and cooperative determination of clock robustness and period. (baudry2010fboxproteinsfkf1 pages 1-2)

5. Annotation-risk assessment (core vs context-specific; misannotation checks)

5.1 Core, high-confidence GO directions (recommended as “core function”)

1. SCF E3 ubiquitin ligase substrate adaptor activity (F-box protein) and related terms: strongly supported by SCF dependence and substrate-directed proteolysis data. (kiba2007targeteddegradationof pages 1-3, harmon2008cul1regulatestoc1 pages 1-2)
2. Regulation of circadian rhythm / determination of circadian period via TOC1/PRR5 turnover: strong genetic and mechanistic evidence including recent quantitative temperature-series data. (maeda2024coldinduceddegradationof pages 7-8, kiba2007targeteddegradationof pages 8-9)
3. Blue light response / blue-light-regulated proteolysis (photoreceptor-coupled turnover): supported by blue-light stabilization and LOV photoreceptor biology. (fujiwara2008posttranslationalregulationof pages 1-2, fujiwara2008novelbluelight pages 1-2)

5.2 Context-specific or higher-risk extensions (annotate cautiously)

1. Direct nuclear localization: while some clock substrates (PRRs) are nuclear-localized, ZTL itself is cytosol-enriched in primary imaging, and its key demonstrated localization function is to alter GI partitioning. CC annotations should avoid “exclusively nuclear”. (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 5-7)
2. HSP90 chaperone complex membership / maturation mechanism: present in review summaries; primary experimental support was not extracted here, so GO annotations implying direct chaperone-client maturation should be added only with direct evidence. (liu2024giganteaunveiledexploring pages 7-8)
3. S6K as a ZTL substrate: ztl-3 affects S6K phosphorylation/abundance rhythms, but direct ZTL–S6K binding/ubiquitination is not established in the excerpt; annotate as an emerging regulatory connection rather than a confirmed direct substrate. (boix202440sribosomalprotein pages 3-4, boix202440sribosomalprotein pages 8-9)
4. Immunity signaling: ZTL–CHE interaction and pathogen effector interference supports clock–immunity crosstalk, but “inflammatory signaling” type annotations are not appropriate for plants. (fu2025apathogeneffector pages 6-7)

5.3 Explicit exclusion of unrelated processes requested

No evidence from the retrieved Arabidopsis ZTL literature supports roles in:
- Apoptosis/developmental cell death programs in the animal sense
- Pyroptosis
- Neuronal functions or synaptic remodeling
- Inflammatory signaling pathways

These terms are animal-centric and should be considered misannotation risks if present. (kiba2007targeteddegradationof pages 1-3, fu2025apathogeneffector pages 6-7)

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

Recent and high-priority (2023–2024)

• Maeda AE et al. (Sep 2024). Cold-induced degradation of core clock proteins implements temperature compensation in the Arabidopsis circadian clock. Science Advances. https://doi.org/10.1126/sciadv.adq0187 (maeda2024coldinduceddegradationof pages 7-8)
• Boix M et al. (May 2024). 40S Ribosomal protein S6 kinase integrates daylength perception and growth regulation in Arabidopsis thaliana. Plant Physiology 195:3039–3052. https://doi.org/10.1093/plphys/kiae254 (boix202440sribosomalprotein pages 3-4, boix202440sribosomalprotein pages 8-9)
• Liu L et al. (Jan 2024). GIGANTEA Unveiled: Exploring Its Diverse Roles and Mechanisms. Genes 15:94. https://doi.org/10.3390/genes15010094 (review; use cautiously for direct mechanistic claims) (liu2024giganteaunveiledexploring pages 7-8)

Recent (2025) mechanistic expansion relevant to substrate scope

• Fu M et al. (Feb 2025). A pathogen effector HaRxL10 hijacks the circadian clock component CHE to perturb both plant development and immunity. Nature Communications 16. https://doi.org/10.1038/s41467-025-56787-w (ZTL–CHE binding evidence; pathogen interference) (fu2025apathogeneffector pages 6-7)

Foundational primary evidence for core function (high-confidence)

• Kiba T et al. (Aug 2007). Targeted Degradation of PSEUDO-RESPONSE REGULATOR5 by an SCF^ZTL Complex Regulates Clock Function and Photomorphogenesis in Arabidopsis thaliana. The Plant Cell 19:2516–2530. https://doi.org/10.1105/tpc.107.053033 (kiba2007targeteddegradationof pages 1-3, kiba2007targeteddegradationof pages 8-9)
• Fujiwara S et al. (Aug 2008). Post-translational Regulation of the Arabidopsis Circadian Clock through Selective Proteolysis and Phosphorylation of PRR Proteins. Journal of Biological Chemistry 283:23073–23083. https://doi.org/10.1074/jbc.m803471200 (phosphorylation-dependent ZTL binding; blue light stabilization; PRR5 substrate) (fujiwara2008posttranslationalregulationof pages 1-2, fujiwara2008posttranslationalregulationof pages 6-6)
• Harmon F et al. (Aug 2008). CUL1 regulates TOC1 protein stability in the Arabidopsis circadian clock. The Plant Journal 55:568–579. https://doi.org/10.1111/j.1365-313x.2008.03527.x (SCF dependence of TOC1 degradation; phenocopy of ztl) (harmon2008cul1regulatestoc1 pages 1-2)
• Baudry A et al. (Mar 2010). F-box proteins FKF1 and LKP2 act in concert with ZEITLUPE to control Arabidopsis clock progression. The Plant Cell 22:606–622. https://doi.org/10.1105/tpc.109.072843 (redundancy among ZTL/FKF1/LKP2; TOC1/PRR5 stabilization) (baudry2010fboxproteinsfkf1 pages 1-2)
• Kim J et al. (Oct 2013). The F-box protein ZEITLUPE controls stability and nucleocytoplasmic partitioning of GIGANTEA. Development 140:4060–4069. https://doi.org/10.1242/dev.096651 (ZTL cytosol enrichment; GI partitioning; LOV-dependent binding; flowering/circadian implications) (kim2013thefboxprotein pages 4-5, kim2013thefboxprotein pages 5-7, kim2013thefboxprotein media fe7aa0b6)
• Song YH et al. (Nov 2014). Distinct roles of FKF1, GI, and ZTL in regulation of CONSTANS stability in photoperiodic flowering. PNAS 111:17672–17677. https://doi.org/10.1073/pnas.1415375111 (ZTL in GI/FKF1/CO network) (song2014distinctrolesof pages 1-2)

Summary artifact

Table: This table summarizes candidate GO-relevant functions, processes, and localizations for Arabidopsis ZTL, distinguishing direct primary evidence from review-level or emerging inferences. It is designed to support annotation review by separating core conserved roles from newer or higher-risk extensions.

References

1. (kiba2007targeteddegradationof pages 1-3): Takatoshi Kiba, Rossana Henriques, H. Sakakibara, and N. Chua. Targeted degradation of pseudo-response regulator5 by an scfztl complex regulates clock function and photomorphogenesis in arabidopsis thaliana[w]. The Plant Cell Online, 19:2516-2530, Aug 2007. URL: https://doi.org/10.1105/tpc.107.053033, doi:10.1105/tpc.107.053033. This article has 321 citations.

2. (kiba2007targeteddegradationof pages 8-9): Takatoshi Kiba, Rossana Henriques, H. Sakakibara, and N. Chua. Targeted degradation of pseudo-response regulator5 by an scfztl complex regulates clock function and photomorphogenesis in arabidopsis thaliana[w]. The Plant Cell Online, 19:2516-2530, Aug 2007. URL: https://doi.org/10.1105/tpc.107.053033, doi:10.1105/tpc.107.053033. This article has 321 citations.

3. (fujiwara2008posttranslationalregulationof pages 6-6): Sumire Fujiwara, Lei Wang, Linqu Han, Sung-Suk Suh, Patrice A. Salomé, C. Robertson McClung, and David E. Somers. Post-translational regulation of the arabidopsis circadian clock through selective proteolysis and phosphorylation of pseudo-response regulator proteins*. Journal of Biological Chemistry, 283:23073-23083, Aug 2008. URL: https://doi.org/10.1074/jbc.m803471200, doi:10.1074/jbc.m803471200. This article has 292 citations and is from a domain leading peer-reviewed journal.

4. (fujiwara2008posttranslationalregulationof pages 1-2): Sumire Fujiwara, Lei Wang, Linqu Han, Sung-Suk Suh, Patrice A. Salomé, C. Robertson McClung, and David E. Somers. Post-translational regulation of the arabidopsis circadian clock through selective proteolysis and phosphorylation of pseudo-response regulator proteins*. Journal of Biological Chemistry, 283:23073-23083, Aug 2008. URL: https://doi.org/10.1074/jbc.m803471200, doi:10.1074/jbc.m803471200. This article has 292 citations and is from a domain leading peer-reviewed journal.

5. (boix202440sribosomalprotein pages 3-4): Marc Boix, Alba Garcia-Rodriguez, Laia Castillo, Bernat Miró, Ferga Hamilton, Sanata Tolak, Adrián Pérez, Carolina Monte-Bello, Camila Caldana, and Rossana Henriques. 40s ribosomal protein s6 kinase integrates daylength perception and growth regulation in arabidopsis thaliana. Plant Physiology, 195:3039-3052, May 2024. URL: https://doi.org/10.1093/plphys/kiae254, doi:10.1093/plphys/kiae254. This article has 8 citations and is from a highest quality peer-reviewed journal.

6. (boix202440sribosomalprotein pages 8-9): Marc Boix, Alba Garcia-Rodriguez, Laia Castillo, Bernat Miró, Ferga Hamilton, Sanata Tolak, Adrián Pérez, Carolina Monte-Bello, Camila Caldana, and Rossana Henriques. 40s ribosomal protein s6 kinase integrates daylength perception and growth regulation in arabidopsis thaliana. Plant Physiology, 195:3039-3052, May 2024. URL: https://doi.org/10.1093/plphys/kiae254, doi:10.1093/plphys/kiae254. This article has 8 citations and is from a highest quality peer-reviewed journal.

7. (kim2013thefboxprotein pages 4-5): Jeongsik Kim, Ruishuang Geng, Richard A. Gallenstein, and David E. Somers. The f-box protein zeitlupe controls stability and nucleocytoplasmic partitioning of gigantea. Development, 140:4060-4069, Oct 2013. URL: https://doi.org/10.1242/dev.096651, doi:10.1242/dev.096651. This article has 124 citations and is from a domain leading peer-reviewed journal.

8. (kim2013thefboxprotein pages 5-7): Jeongsik Kim, Ruishuang Geng, Richard A. Gallenstein, and David E. Somers. The f-box protein zeitlupe controls stability and nucleocytoplasmic partitioning of gigantea. Development, 140:4060-4069, Oct 2013. URL: https://doi.org/10.1242/dev.096651, doi:10.1242/dev.096651. This article has 124 citations and is from a domain leading peer-reviewed journal.

9. (kim2013thefboxprotein media fe7aa0b6): Jeongsik Kim, Ruishuang Geng, Richard A. Gallenstein, and David E. Somers. The f-box protein zeitlupe controls stability and nucleocytoplasmic partitioning of gigantea. Development, 140:4060-4069, Oct 2013. URL: https://doi.org/10.1242/dev.096651, doi:10.1242/dev.096651. This article has 124 citations and is from a domain leading peer-reviewed journal.

10. (maeda2024coldinduceddegradationof pages 7-8): Akari E. Maeda, Hiromi Matsuo, Tomoaki Muranaka, and Norihito Nakamichi. Cold-induced degradation of core clock proteins implements temperature compensation in the arabidopsis circadian clock. Science Advances, Sep 2024. URL: https://doi.org/10.1126/sciadv.adq0187, doi:10.1126/sciadv.adq0187. This article has 15 citations and is from a highest quality peer-reviewed journal.

11. (fu2025apathogeneffector pages 6-7): Mengyao Fu, Yaoyu Zhou, Xin Zhang, Keyi Yang, Yufeng Xu, Xingwei Wang, Zhaodan Chen, Yu Wang, Yabo Shi, Lin Ma, Hanguang Liu, Yuhua Deng, Shujing Cheng, Jinfang Chu, Jingyi Song, Tongjun Sun, Yuanchao Wang, Wei Wang, and Mian Zhou. A pathogen effector harxl10 hijacks the circadian clock component che to perturb both plant development and immunity. Nature Communications, Feb 2025. URL: https://doi.org/10.1038/s41467-025-56787-w, doi:10.1038/s41467-025-56787-w. This article has 22 citations and is from a highest quality peer-reviewed journal.

12. (harmon2008cul1regulatestoc1 pages 1-2): Frank Harmon, Takato Imaizumi, and William M. Gray. Cul1 regulates toc1 protein stability in the arabidopsis circadian clock. The Plant journal : for cell and molecular biology, 55 4:568-79, Aug 2008. URL: https://doi.org/10.1111/j.1365-313x.2008.03527.x, doi:10.1111/j.1365-313x.2008.03527.x. This article has 61 citations.

13. (suetsugu2013evolutionofthree pages 7-8): Noriyuki Suetsugu and Masamitsu Wada. Evolution of three lov blue light receptor families in green plants and photosynthetic stramenopiles: phototropin, ztl/fkf1/lkp2 and aureochrome. Plant & cell physiology, 54 1:8-23, Dec 2013. URL: https://doi.org/10.1093/pcp/pcs165, doi:10.1093/pcp/pcs165. This article has 175 citations and is from a domain leading peer-reviewed journal.

14. (kiba2007targeteddegradationof pages 11-12): Takatoshi Kiba, Rossana Henriques, H. Sakakibara, and N. Chua. Targeted degradation of pseudo-response regulator5 by an scfztl complex regulates clock function and photomorphogenesis in arabidopsis thaliana[w]. The Plant Cell Online, 19:2516-2530, Aug 2007. URL: https://doi.org/10.1105/tpc.107.053033, doi:10.1105/tpc.107.053033. This article has 321 citations.

15. (kim2013thefboxprotein pages 7-8): Jeongsik Kim, Ruishuang Geng, Richard A. Gallenstein, and David E. Somers. The f-box protein zeitlupe controls stability and nucleocytoplasmic partitioning of gigantea. Development, 140:4060-4069, Oct 2013. URL: https://doi.org/10.1242/dev.096651, doi:10.1242/dev.096651. This article has 124 citations and is from a domain leading peer-reviewed journal.

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