The research report should be a detailed narrative explaining the function, biological processes, and localization of the gene product. Citations should be given for all claims.
You should prioritize authoritative reviews and primary scientific literature when conducting research. You can supplement
this with annotations you find in gene/protein databases, but these can be outdated or inaccurate.
We are specifically interested in the primary function of the gene - for enzymes, what reaction is catalyzed, and what is the substrate specificity? For transporters, what is the substrate? For structural proteins or adapters, what is the broader structural role? For signaling molecules, what is the role in the pathway.
We are interested in where in or outside the cell the gene product carries out its function.
We are also interested in the signaling or biochemical pathways in which the gene functions. We are less interested in broad pleiotropic effects, except where these elucidate the precise role.
Include evidence where possible. We are interested in both experimental evidence as well as inference from structure, evolution, or bioinformatic analysis. Precise studies should be prioritized over high-throughput, where available.
GID1B is a soluble gibberellin (GA) receptor, not an established GA-metabolizing enzyme. The target is Arabidopsis thaliana GID1B, locus At3g63010; the supplied UniProt record identifies accession Q9LYC1 and the aliases CXE14 and GID1L2. A primary publication independently maps Arabidopsis GID1b to At3g63010 and distinguishes it from GID1a (At3g05120), GID1c (At5g27320), and rice GID1. Thus, the evidence below concerns the requested Arabidopsis protein rather than a similarly named receptor from another species. (ueguchitanaka2007molecularinteractionsof pages 15-16)
GID1B has a carboxylesterase/hormone-sensitive-lipase-like α/β-hydrolase fold, consistent with the AB-hydrolase and GDXG-family domains specified in the supplied UniProt description. It retains characteristic HGG and GXSXG motifs, but the histidine required for the conventional lipase catalytic triad is replaced in GID1 receptors. No established substrate-hydrolysis reaction, catalytic product, or physiologically relevant carboxylesterase activity can therefore be assigned to GID1B. Its experimentally supported molecular activity is selective hormone binding followed by DELLA-repressor binding; “carboxylesterase 14” describes its sequence ancestry, not a demonstrated catalytic function. (sun2008gibberellinmetabolismperception pages 12-14, sun2008gibberellinmetabolismperception pages 14-15, yoshida2018evolutionanddiversification pages 1-2)
Bioactive GAs, particularly GA₄, are receptor ligands. Work on the GID1 family identifies GA₁ and GA₃ as other bioactive ligands and distinguishes these from inactive derivatives such as GA₉ and GA₃₄; the detailed ligand comparisons in that evolutionary study were made largely with rice and Selaginella receptors and must not be read as an Arabidopsis-GID1B-specific affinity series. Structural features associated with bioactivity include a C3 hydroxyl, C6 carboxyl, and appropriate lactone and C2 substitutions. GA binding occurs in a pocket corresponding to the ancestral esterase active-site region. An amino-terminal movable “lid” closes over bound GA and forms a surface that recruits a DELLA protein. The best-characterized Arabidopsis receptor–DELLA crystal structure uses GID1A, so its atomic details provide a mechanistic model for, rather than an isoform-specific structure of, GID1B. (yoshida2018evolutionanddiversification pages 3-4, yoshida2018evolutionanddiversification pages 1-2, yoshida2018evolutionanddiversification pages 4-5, shani2024highlightsingibberellin pages 7-8)
GID1B-specific quantitative evidence is unusually strong for GA₄. Surface-plasmon-resonance measurements gave Arabidopsis GID1B–GA₄ association and dissociation rate constants of 1.9 × 10⁴ M⁻¹ s⁻¹ and 6.9 × 10⁻⁴ s⁻¹, respectively. Their ratio gives an approximately 36 nM calculated dissociation constant, versus approximately 0.86 µM calculated for GID1A under the same comparison. The principal difference was GA₄ dissociating approximately 17-fold more slowly from GID1B. In a separate GA₄-dependent yeast assay measuring receptor interaction with the Arabidopsis DELLA protein GAI, the EC₅₀ was 3.2 nM for GID1B, versus 180 nM for GID1A—approximately 60-fold greater assay sensitivity. An interaction-assay EC₅₀ is not a purified-protein binding constant and should not be substituted for the SPR-derived value. (yamamoto2010aricegid1 pages 6-9, yoshida2018evolutionanddiversification pages 4-5)
GID1B also differs from its Arabidopsis paralogs in showing detectable GAI interaction without added GA in yeast. Substitution of its distinctive loop with the GID1A loop abolished this hormone-independent interaction while retaining GA-dependent binding, implicating receptor conformation in the difference. This is not evidence that normal plant signaling is entirely hormone-independent: co-immunoprecipitation from Arabidopsis seedlings expressing FLAG–GID1B showed that association with the DELLA protein RGA increases with GA₃ concentration. (yamamoto2010aricegid1 pages 6-9, ariizumi2008proteolysisindependentdownregulationof pages 5-6)
GA-bound GID1 recruits DELLA repressors, including GAI and RGA, into a signaling complex. In the canonical Arabidopsis pathway, this facilitates recognition by the SCF^SLY1 ubiquitin ligase and subsequent DELLA degradation by the 26S proteasome, releasing DELLA-imposed restrictions on transcriptional regulators. Arabidopsis lacking all three GID1 receptors fails to execute the examined GA-dependent DELLA-degradation and transcriptional responses, whereas individual receptors can partly compensate for one another. GID1B binding can additionally weaken DELLA repression without DELLA destruction: GID1 overexpression, including GID1B overexpression, restored growth in sly1 mutants without a corresponding reduction in accumulated RGA; GA-biosynthesis inhibition blocked that growth rescue. This genetic result establishes a proteolysis-independent route but does not, by itself, specify the complete physical interface used by GID1B. (willige2007thedelladomain pages 8-9, ariizumi2008proteolysisindependentdownregulationof pages 2-4, ariizumi2008proteolysisindependentdownregulationof pages 5-6)
The most distinctive physiological contribution supported for GID1B is sensitive GA perception in roots. Its transcript is relatively root-enriched, and in experiments limiting GA biosynthesis, gid1b single-mutant roots were more inhibited and less responsive to GA₄ rescue than wild type or the other single-receptor mutants; hypocotyl responses were comparatively similar. At 16 °C, gid1b root growth was impaired more than that of the other receptor single mutants relative to growth at 22 °C. These observations support a contribution to root elongation when GA availability or temperature limits growth. Higher ligand affinity is a plausible contributor, but receptor abundance, hormone distribution, and downstream components could also contribute; the experiments do not isolate affinity as the sole cause. (tanimoto2012tallorshort? pages 6-7, yoshida2018evolutionanddiversification pages 7-8, yoshida2018evolutionanddiversification pages 6-7)
GID1B also contributes to seed-germination responsiveness and vegetative growth, although paralog redundancy matters: loss of GID1B reduced GA sensitivity in a germination assay, while the three-receptor mutant has a much more severe germination defect and requires seed-coat removal to germinate under reported conditions. Consequently, severe whole-plant defects of the triple mutant cannot be assigned uniquely to GID1B. (ariizumi2008proteolysisindependentdownregulationof pages 2-4, willige2007thedelladomain pages 4-6)
The relevant site of action is intracellular, with nuclear signaling central to its DELLA interaction. GID1–GFP observations support localization of Arabidopsis GID1 receptors in both cytoplasm and nucleus, and GID1A–GFP was directly observed in both compartments. The retrieved microscopy does not establish an independently measured cytoplasm-to-nucleus distribution for GID1B itself. Its physical association with RGA in plant extracts and the nuclear role of DELLA repressors nevertheless support a nuclear functional site; there is no basis here for assigning GID1B an extracellular or membrane-receptor function. (sun2008gibberellinmetabolismperception pages 12-14, willige2007thedelladomain pages 4-6, sun2011themolecularmechanism pages 3-4, ariizumi2008proteolysisindependentdownregulationof pages 5-6)
The following table separates direct GID1B measurements from family-level inference and lists important assay limitations. (yoshida2018evolutionanddiversification pages 4-5, willige2007thedelladomain pages 4-6, huang2024phosphorylationactivatesmaster pages 5-7, yamamoto2010aricegid1 pages 6-9)
| Evidence tier | GID1B-specific finding | Method / quantitative result | Interpretation and limitation | Source |
|---|---|---|---|---|
| Direct biochemical | AtGID1B binds bioactive GA₄ with substantially higher affinity than AtGID1A. | Purified-protein SPR: AtGID1B kₐ = 1.9 × 10⁴ M⁻¹ s⁻¹ and kᵈ = 6.9 × 10⁻⁴ s⁻¹; calculated KD = kᵈ/kₐ ≈ 3.6 × 10⁻⁸ M (36 nM). Corresponding calculated AtGID1A KD ≈ 8.6 × 10⁻⁷ M (0.86 µM). | The ∼24-fold affinity difference chiefly reflects AtGID1B’s ∼17-fold slower GA₄ dissociation. Both KD values are calculated from reported kinetic constants rather than quoted equilibrium values. | Yamamoto et al., 2010, Plant Cell (yamamoto2010aricegid1 pages 6-9) |
| Direct interaction assay | GA₄ drives AtGID1B interaction with the Arabidopsis DELLA protein GAI at much lower concentrations than for AtGID1A. | Yeast two-hybrid dose response: AtGID1B–GAI EC₅₀ = 3.2 × 10⁻⁹ M versus AtGID1A–GAI EC₅₀ = 1.8 × 10⁻⁷ M, an approximately 60-fold difference. | EC₅₀ measures ternary-complex assay response and is not an equilibrium receptor–ligand KD; it should not be numerically equated with the SPR result. | Yoshida et al., 2018, PNAS (yoshida2018evolutionanddiversification pages 4-5) |
| Direct mechanistic | AtGID1B can interact detectably with GAI without added GA, unlike AtGID1A and AtGID1C under the tested conditions. | Yeast two-hybrid and loop-swap/mutagenesis: replacing the AtGID1B β2–β3-region loop with the AtGID1A loop abolished hormone-independent interaction while preserving GA-dependent interaction. | Supports an atypically primed/partly closed receptor conformation. This does not mean that normal in-planta signaling is GA-independent; GA strongly enhances GID1B–DELLA association. | Yamamoto et al., 2010, Plant Cell (yamamoto2010aricegid1 pages 1-2, yamamoto2010aricegid1 pages 6-9) |
| Direct in vivo interaction | GID1B associates with the DELLA repressor RGA in planta in a GA-concentration-dependent manner. | Co-immunoprecipitation from Arabidopsis expressing FLAG:GID1B showed increasing recovered RGA with increasing GA₃ treatment. | Confirms receptor–DELLA complex formation in plant tissue; the experiment tested GA₃-dependent association rather than direct GA₄ affinity. | Ariizumi et al., 2008, Plant Cell (ariizumi2008proteolysisindependentdownregulationof pages 5-6) |
| Direct physiological / genetic | GID1B is particularly important for root growth when GA availability is limited and at low temperature. | Under GA-biosynthesis inhibition, single gid1b roots were more inhibited and less responsive to GA₄ rescue than wild type or the other single-receptor mutants, whereas hypocotyl responses were similar. At 16 °C versus 22 °C, gid1b root growth was impaired more strongly; 15 seedlings were measured per treatment. | Supports root-biased, high-sensitivity GA perception by GID1B. The data do not establish that affinity alone explains the organ- and temperature-specific phenotype. | Yoshida et al., 2018, PNAS (yoshida2018evolutionanddiversification pages 7-8, yoshida2018evolutionanddiversification pages 6-7, yoshida2018evolutionanddiversification pages 8-9) |
| Direct regulatory, recent | GID1B is an RGA-activated feedback target whose chromatin regulation depends on DELLA phosphorylation and histone H2A association. | Arabidopsis ChIP-qPCR included the GID1B promoter: non-phosphorylatable RGA-m2A had reduced target-promoter occupancy, while phosphomimetic RGA-m2D resembled wild-type RGA; expression changes were consistent with reduced activation of GID1B by RGA-m2A. | Places GID1B in negative feedback/homeostatic control of GA signaling. The reported excerpt does not supply a GID1B-specific fold change or absolute occupancy value. | Huang et al., 2024, Nature Communications (huang2024phosphorylationactivatesmaster pages 5-7, huang2024phosphorylationactivatesmaster pages 7-9, huang2024phosphorylationactivatesmaster pages 1-2) |
| Family-level / indirect for isoform | Arabidopsis GID1 receptors are soluble intracellular proteins found in the cytoplasm and nucleus. | GID1–GFP family-level reports and direct GID1A–GFP imaging detected both compartments; GID1A localization was unchanged by GA or GA-biosynthesis inhibition. | Supports cytosolic and nuclear action for the receptor family, especially nuclear DELLA regulation, but the retrieved evidence does not document isoform-specific GID1B–GFP microscopy. | Sun, 2008, The Arabidopsis Book; Willige et al., 2007, Plant Cell (sun2008gibberellinmetabolismperception pages 12-14, willige2007thedelladomain pages 4-6, sun2011themolecularmechanism pages 3-4) |
Table: Evidence specific to Arabidopsis GID1B (Q9LYC1/At3g63010), separated from family-level inference. Quantitative affinity, interaction, physiology, feedback regulation, and localization claims are qualified by their experimental limits.
A September 2024 Arabidopsis study extended the homeostatic model upstream of the receptor: the DELLA protein RGA associates with the GID1B promoter, and phosphorylation that strengthens RGA binding to histone H2A increased its association with target chromatin. A phosphorylation-defective RGA variant showed reduced promoter occupancy and reduced activation of RGA-induced genes, including GID1B. This places GID1B expression within a feedback circuit linking DELLA activity to GA perception; it is evidence about regulation of the GID1B gene, not a newly discovered enzymatic activity of its protein. The 2023 bioRxiv version was subsequently superseded by this published 2024 study. (huang2024phosphorylationactivatesmaster pages 5-7, huang2024phosphorylationactivatesmaster pages 7-9, huang2023phosphorylationpromotesdella pages 20-24)
The authoritative 2024 synthesis by Shani, Hedden, and Sun continues to identify the soluble GID1–DELLA–SLY1 module as the central GA-perception pathway, while emphasizing additional regulation of DELLA activity and GA homeostasis. A May 2024 research implementation used an engineered, fluorescence-ratio DELLA/RGA biosensor to map GA-signaling activity at the Arabidopsis shoot apical meristem and relate it to internode specification. It reports pathway activity influenced by GA perception; the biosensor is modified RGA, not GID1B, and its spatial measurements are not a direct localization map of GID1B protein. (shani2024highlightsingibberellin pages 10-11, shani2024highlightsingibberellin pages 8-10, shi2024aquantitativegibberellin pages 6-8, shi2024aquantitativegibberellin pages 2-3)
For structural context beyond the requested 2023–2024 priority, an August 2025 cryo-EM study resolved Arabidopsis GA₃–GID1A–RGA and GA₃–GID1A–RGA–SLY1–ASK1 assemblies and proposed how receptor binding can inhibit DELLA interaction with IDD transcription factors without proteolysis. This sharpens the pathway model but is GID1A evidence, not a solved GID1B complex. In practical terms, GID1B’s demonstrated high sensitivity and root-biased function make receptor specialization a plausible subject for growth-regulator and plant-engineering research. The cited work establishes experimental assays and physiological effects in Arabidopsis; it does not establish a commercially implemented crop variety or agronomic product engineered specifically through Arabidopsis GID1B. (dahal2025structuralinsightsinto pages 1-2, yoshida2018evolutionanddiversification pages 7-8, yoshida2018evolutionanddiversification pages 6-7)
References
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(dahal2025structuralinsightsinto pages 1-2): Pawan Dahal, Yan Wang, Jianhong Hu, Jeongmoo Park, Karly Forker, Zhong-Lin Zhang, Kedar Sharma, Mario J. Borgnia, Tai-ping Sun, and Pei Zhou. Structural insights into proteolysis-dependent and -independent suppression of the master regulator della by the gibberellin receptor. Proceedings of the National Academy of Sciences of the United States of America, 122 32:e2511012122, Aug 2025. URL: https://doi.org/10.1073/pnas.2511012122, doi:10.1073/pnas.2511012122. This article has 22 citations and is from a highest quality peer-reviewed journal.