GID1B (GA INSENSITIVE DWARF1B; locus At3g63010) is one of three soluble gibberellin (GA) receptors in Arabidopsis thaliana, together with GID1A and GID1C. Like its paralogs it has the alpha/beta-hydrolase fold of the hormone-sensitive lipase (GDXG) family but is not a hydrolase; the fold forms a pocket that binds bioactive GAs, after which an N-terminal lid closes over the hormone and creates a surface that binds the N-terminal DELLA domain of the DELLA growth repressors (GAI, RGA, RGL1, RGL2, RGL3). The GA-GID1-DELLA complex is recognized by the SCF(SLY1) E3 ubiquitin ligase, leading to DELLA polyubiquitination and proteasomal degradation; GA-GID1 binding can also inhibit DELLA activity without proteolysis. GID1B differs biochemically from GID1A and GID1C: it has about ten-fold higher affinity for GA4, binds GA over a narrow pH range, and needs less GA to engage DELLAs, suggesting it acts as a receptor at low GA levels. GID1B belongs to a separate eudicot GID1b clade and is expressed mainly in ovules, seeds and roots, where it contributes to GA-dependent root growth when GA is limiting; its transcript rises during seed after-ripening, and its overexpression relieves DELLA repression of germination. Single gid1b mutants have no obvious phenotype, but GID1B contributes, redundantly with GID1A, to stamen elongation, male fertility and seed set, and the gid1a gid1b gid1c triple mutant is a GA-insensitive dwarf.
Definition: Binding to a gibberellin and, as a result, undergoing a conformational change that promotes gibberellin-dependent binding of DELLA repressor proteins, thereby transducing the gibberellin signal.
Justification: GID1 proteins, including GID1B, are bona fide soluble GA receptors but GO has no gibberellin receptor activity term (checked in GO via OAK/OLS); gibberellin binding (GO:0010331) captures ligand binding but not signal transduction. Same proposal as in the GID1A review.
Supporting Evidence:
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL2 (Q8GXW1). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:16709201 A two-hybrid yeast system only showed in vivo interaction in the presence of GA(4) between each AtGID1 and the Arabidopsis DELLA proteins (AtDELLAs), negative regulators of GA signaling |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:16709201 A two-hybrid yeast system only showed in vivo interaction in the presence of GA(4) between each AtGID1 and the Arabidopsis DELLA proteins (AtDELLAs), negative regulators of GA signaling |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:16709201 A two-hybrid yeast system only showed in vivo interaction in the presence of GA(4) between each AtGID1 and the Arabidopsis DELLA proteins (AtDELLAs), negative regulators of GA signaling |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:16709201 A two-hybrid yeast system only showed in vivo interaction in the presence of GA(4) between each AtGID1 and the Arabidopsis DELLA proteins (AtDELLAs), negative regulators of GA signaling |
| GO:0005515 protein binding | IPI PMID:16709201 Identification and characterization of Arabidopsis gibberell... | REMOVE | Summary: Interaction of GID1B with the F-box protein SLY1/GID2 (Q9STX3), detected in yeast multi-hybrid assays where DELLA bridges GA-GID1 to SLY1. Reason: Generic protein binding is uninformative; the GID1-SLY1 association is likely bridged by DELLA within the GA-GID1-DELLA-SCF(SLY1) complex rather than a direct activity of the receptor. Removal does not mean the reported association is false. Supporting Evidence: PMID:16709201 A two-hybrid yeast system only showed in vivo interaction in the presence of GA(4) between each AtGID1 and the Arabidopsis DELLA proteins (AtDELLAs), negative regulators of GA signaling |
| GO:0005515 protein binding | IPI PMID:17194763 Genetic characterization and functional analysis of the GID1... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:17194763 GA enhances the interaction between GID1 and DELLA proteins |
| GO:0005515 protein binding | IPI PMID:17194763 Genetic characterization and functional analysis of the GID1... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:17194763 GA enhances the interaction between GID1 and DELLA proteins |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL3 (Q9LF53). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18216856 Coordinated regulation of Arabidopsis thaliana development b... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005515 protein binding | IPI PMID:18827182 Proteolysis-independent downregulation of DELLA repression i... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18827182 Since DELLA shows increasing interaction with GID1 with increasing GA levels |
| GO:0005515 protein binding | IPI PMID:18827182 Proteolysis-independent downregulation of DELLA repression i... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:18827182 Since DELLA shows increasing interaction with GID1 with increasing GA levels |
| GO:0005515 protein binding | IPI PMID:19429606 FRIGIDA delays flowering in Arabidopsis via a cotranscriptio... | REMOVE | Summary: IntAct IPI interaction of GID1B with RGA attributed to a FRIGIDA/cap-binding-complex flowering paper. The cached full text does not mention GID1 or DELLA proteins, so the source of this row cannot be verified here. Reason: Generic protein binding is uninformative and is removed under the protein-binding policy. The GID1B-RGA interaction itself is real (GA-dependent binding shown in PMID:16709201 and PMID:17194763) and is already covered by gibberellin binding (GO:0010331), the GA signaling process terms and the proposed gibberellin receptor activity term. Separately, the cited reference looks mismatched: the cached full text of PMID:19429606 (FRIGIDA and the nuclear cap-binding complex) does not mention GID1 or DELLA proteins, so this is probably an IntAct reference error. Removal does not mean the interaction is false. Supporting Evidence: PMID:19429606 FRIGIDA delays flowering in Arabidopsis via a cotranscriptional mechanism involving direct interaction with the nuclear cap-binding complex |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL2 (Q8GXW1). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:19500306 Differential expression and affinities of Arabidopsis gibber... | REMOVE | Summary: Interaction of GID1B with the F-box protein SLY1/GID2 (Q9STX3), detected in yeast multi-hybrid assays where DELLA bridges GA-GID1 to SLY1. Reason: Generic protein binding is uninformative; the GID1-SLY1 association is likely bridged by DELLA within the GA-GID1-DELLA-SCF(SLY1) complex rather than a direct activity of the receptor. Removal does not mean the reported association is false. Supporting Evidence: PMID:19500306 We then evaluated the affinity of the AtGID1-DELLA interaction by a competitive yeast three-hybrid system and also by QCM apparatus |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (O64688) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL2 (Q8GXW1). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q8LF89) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q9C6Z3) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL1 (Q9C8Y3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q9FMT4) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q9FVU9) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGL3 (Q9LF53). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein GAI (Q9LQT8). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q9M872) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q9S7U7) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: High-throughput yeast two-hybrid interaction of GID1B with a non-DELLA protein (Q9SG92) from the phytohormone interactome map. Reason: Generic protein binding from a large-scale screen, with no follow-up establishing a function for this partner in GA perception. Uninformative; removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005515 protein binding | IPI PMID:32612234 Extensive signal integration by the phytohormone protein net... | REMOVE | Summary: GA-dependent interaction of GID1B with the DELLA protein RGA (Q9SLH3). This interaction is the effector step of the receptor, but generic protein binding conveys no functional information. Reason: Generic protein binding is uninformative. The underlying GA-dependent GID1-DELLA interaction is real and central to receptor function, but it is captured by gibberellin binding (GO:0010331) plus the GA signaling process terms and the proposed gibberellin receptor activity term; no existing GO MF term specifically describes DELLA binding by an activated receptor. Removal does not mean the interaction is false. Supporting Evidence: PMID:32612234 we experimentally generated a systems-level map of the Arabidopsis phytohormone signalling network, consisting of more than 2,000 binary protein-protein interactions |
| GO:0005634 nucleus | IBA GO_REF:0000033 | ACCEPT | Summary: Nuclear localization of GID1B (IBA), consistent with GID1 being a soluble nuclear receptor that engages nuclear DELLA repressors. Reason: GID1 receptors act in the nucleus where DELLA proteins reside; consistent with UniProt (by similarity), the GID1 clade IBA and GA-GID1-DELLA interaction in the nucleus. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005634 nucleus | IEA GO_REF:0000044 | ACCEPT | Summary: Nuclear localization of GID1B (IEA), consistent with GID1 being a soluble nuclear receptor that engages nuclear DELLA repressors. Reason: GID1 receptors act in the nucleus where DELLA proteins reside; consistent with UniProt (by similarity), the GID1 clade IBA and GA-GID1-DELLA interaction in the nucleus. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005634 nucleus | ISM GO_REF:0000122 | ACCEPT | Summary: Nuclear localization of GID1B (ISM), consistent with GID1 being a soluble nuclear receptor that engages nuclear DELLA repressors. Reason: GID1 receptors act in the nucleus where DELLA proteins reside; consistent with UniProt (by similarity), the GID1 clade IBA and GA-GID1-DELLA interaction in the nucleus. Supporting Evidence: PMID:18216856 In the presence of GA, GID1 proteins (GA receptors) elevate their direct interaction with DELLA proteins in the nucleus |
| GO:0005737 cytoplasm | IBA GO_REF:0000033 | KEEP AS NON CORE | Summary: Cytoplasmic pool inferred from the GID1 clade (experimental nucleocytoplasmic localization of GID1A). Reason: GID1 proteins are soluble receptors distributed between nucleus and cytoplasm (GID1A-GFP is nucleocytoplasmic), so the clade IBA is plausible and not contradicted for this paralog. However, the nuclear pool is the functionally relevant one, where the GA-GID1 complex engages nuclear DELLA repressors; no cytoplasm-specific role is known, so the location is kept as non-core (consistent with the SLY1 review). Supporting Evidence: file:ARATH/GID1B/GID1B-deep-research-falcon.md Arabidopsis GID1 receptors are soluble intracellular proteins found in the cytoplasm and nucleus. file:ARATH/GID1A/GID1A-deep-research-falcon.md GFP-tagged Arabidopsis GID1A localized to both nucleus and cytoplasm, and this distribution was not altered by GA or paclobutrazol treatment. |
| GO:0009739 response to gibberellin | IEP PMID:17933900 Global analysis of della direct targets in early gibberellin... | ACCEPT | Summary: GID1B transcript is regulated by GA/DELLA feedback (expression-pattern evidence). Reason: GID1 receptor genes are direct DELLA feedback targets, consistent with involvement in GA responses; redundant with the stronger receptor/signaling annotations. Supporting Evidence: PMID:17933900 they help establish GA homeostasis by direct feedback regulation on the expression of GA biosynthetic and GA receptor genes |
| GO:0009739 response to gibberellin | IGI PMID:18827182 Proteolysis-independent downregulation of DELLA repression i... | ACCEPT | Summary: Genetic evidence (in combination with the GA1/ga1-3 locus and sly1 backgrounds): GID1B overexpression relieves DELLA repression in a GA-dependent way. Reason: Consistent with the receptor role in GA responses, including the proteolysis-independent inhibition of DELLA by GA-GID1. Supporting Evidence: PMID:18827182 GID1 overexpression rescued the sly1 dwarf and infertility phenotypes without decreasing the accumulation of the DELLA protein PMID:18827182 GA-bound GID1 can block DELLA repressor activity by direct protein-protein interaction with the DELLA domain |
| GO:0009739 response to gibberellin | IGI NOT PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | REMOVE | Summary: NOT involved in response to gibberellin (IGI, with Q940G6), based on the absence of a pistil/fruit phenotype in a gid1b single or double mutant in which another GID1 paralog remains. Reason: The negation is contradicted by direct evidence that GID1B is a functional GA receptor: recombinant GID1B binds GA and interacts with DELLAs only in the presence of GA, and it rescues the rice gid1 mutant. Lack of a phenotype in a mutant retaining a redundant paralog (the paper itself reports compensatory GID1A up-regulation) reflects genetic redundancy, not absence of involvement in GA responses. Supporting Evidence: PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis PMID:24961590 Elimination of two out of the three GA receptors in each double mutant combination may cause up-regulated expression of the remaining GID1 gene, which may alleviate reduced GA-response phenotype |
| GO:0009739 response to gibberellin | IGI NOT PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | REMOVE | Summary: NOT involved in response to gibberellin (IGI, with Q9MAA7), based on the absence of a pistil/fruit phenotype in a gid1b single or double mutant in which another GID1 paralog remains. Reason: The negation is contradicted by direct evidence that GID1B is a functional GA receptor: recombinant GID1B binds GA and interacts with DELLAs only in the presence of GA, and it rescues the rice gid1 mutant. Lack of a phenotype in a mutant retaining a redundant paralog (the paper itself reports compensatory GID1A up-regulation) reflects genetic redundancy, not absence of involvement in GA responses. Supporting Evidence: PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis PMID:24961590 Elimination of two out of the three GA receptors in each double mutant combination may cause up-regulated expression of the remaining GID1 gene, which may alleviate reduced GA-response phenotype |
| GO:0009739 response to gibberellin | IMP NOT PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | REMOVE | Summary: NOT involved in response to gibberellin (IMP), based on the absence of a pistil/fruit phenotype in a gid1b single or double mutant in which another GID1 paralog remains. Reason: The negation is contradicted by direct evidence that GID1B is a functional GA receptor: recombinant GID1B binds GA and interacts with DELLAs only in the presence of GA, and it rescues the rice gid1 mutant. Lack of a phenotype in a mutant retaining a redundant paralog (the paper itself reports compensatory GID1A up-regulation) reflects genetic redundancy, not absence of involvement in GA responses. Supporting Evidence: PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis PMID:24961590 Elimination of two out of the three GA receptors in each double mutant combination may cause up-regulated expression of the remaining GID1 gene, which may alleviate reduced GA-response phenotype |
| GO:0010331 gibberellin binding | IBA GO_REF:0000033 | ACCEPT | Summary: GID1B binds bioactive gibberellins (highest affinity for GA4); IBA inferred from the GID1 clade (PTN000546395) seeded by Arabidopsis GID1A and rice GID1, and directly supported by in vitro GA-binding assays on recombinant GID1B. Reason: Core molecular function of a GA receptor. GID1B lies within the GID1 receptor clade, and its own GA-binding activity was demonstrated biochemically. Supporting Evidence: PMID:16709201 The GA-binding activities of the three recombinant proteins were confirmed by an in vitro assay PMID:16709201 These results demonstrate that all three AtGID1s functioned as GA receptors in Arabidopsis PMID:16709201 AtGID1b was unique in its binding affinity to GA(4) and in its pH dependence when compared with the other two |
| GO:0010476 gibberellin mediated signaling pathway | IGI PMID:17521411 Multiple loss-of-function of Arabidopsis gibberellin recepto... | ACCEPT | Summary: The gid1a gid1b gid1c triple mutant completely loses GA responsiveness, placing all three GID1 receptors in the GA-mediated signaling pathway. Reason: Core process: GID1B is one of the three redundant GA receptors that initiate GA signaling. Supporting Evidence: PMID:17521411 the triple knockout seedlings completely lost their ability to respond to exogenously applied GA PMID:17194763 GID1a, GID1b, and GID1c function as positive regulators of the GA-signaling cascade in Arabidopsis |
| GO:0010629 negative regulation of gene expression | IGI PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | MARK AS OVER ANNOTATED | Summary: Genetic interaction annotation from PMID:24961590: in a double mutant lacking GID1B and its paralog (Q940G6), expression of the remaining GID1A receptor gene was enhanced. Reason: The observation reflects indirect GA/DELLA homeostatic feedback on GID1A transcription when receptor capacity is reduced, not a gene-expression regulatory activity of the receptor itself. The broad term "negative regulation of gene expression" overstates the evidence. Supporting Evidence: PMID:24961590 The up-regulation of GID1A in gid1b gid1c may be consequence of this feedback mechanism |
| GO:0016787 hydrolase activity | IBA GO_REF:0000033 | REMOVE | Summary: Hydrolase activity propagated by IBA from a deep PAINT node (PTN009058710) seeded by catalytically active carboxylesterases/arylacetamide deacetylases that share the alpha/beta-hydrolase (HSL/GDXG lipolytic enzyme) fold. Reason: GID1 receptors retain the hormone-sensitive-lipase fold but are not hydrolases; the fold has been repurposed into a GA-binding pocket. The GID1 clade diverged from the catalytic ancestral function, so the deep-node IBA and the fold-based IEA are over-propagated to a non-catalytic receptor (pseudoenzyme over-annotation). Propagation Review Root cause: PROPAGATION BAD Failure modes: PSEUDO OR SUBACTIVITY LOSS FUNCTIONAL DIVERGENCE Sources checked: PANTHER:PTN009058710 · PTN009058710 SUPPORTS SOURCE BUT NOT TARGET Deep PTHR23024 node seeded by catalytically active carboxylesterases/arylacetamide deacetylases (e.g. AT1G49660, AT5G23530, human/mouse AADAC-like, bacterial esterases). The GID1 receptor subclade nested within it has lost hydrolase activity and was repurposed for GA binding; the IBD should carry a NOT/loss at the GID1 clade node. Supporting Evidence: PMID:24961590 GID1 was first described in rice as a nuclear localized protein similar to hormone-sensitive lipase family without hydrolase activity |
| GO:0016787 hydrolase activity | IEA GO_REF:0000002 | REMOVE | Summary: Hydrolase activity assigned by InterPro2GO mapping (IEA) from the alpha/beta-hydrolase (HSL/GDXG lipolytic enzyme) fold signatures IPR002168 and IPR013094. Reason: GID1 receptors retain the hormone-sensitive-lipase fold but are not hydrolases; the fold has been repurposed into a GA-binding pocket. The GID1 clade diverged from the catalytic ancestral function, so the fold-based InterPro mapping over-propagates hydrolase activity to a non-catalytic receptor (pseudoenzyme over-annotation). Supporting Evidence: PMID:24961590 GID1 was first described in rice as a nuclear localized protein similar to hormone-sensitive lipase family without hydrolase activity |
| GO:0048530 fruit morphogenesis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: ARBA-predicted role in fruit morphogenesis, a downstream developmental output of GA signaling. Reason: GA perception by the GID1 receptors (partially redundantly, with GID1A predominant) controls fruit growth; GID1B contributes mainly through ovule/seed development. Pleiotropic downstream output, not the core function. Supporting Evidence: PMID:24961590 We show that GID1A plays a major role during fruit-set, whereas GID1B and GID1C have partially redundant function with GID1A in seed development and pod elongation, respectively |
| GO:0048530 fruit morphogenesis | IGI PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | KEEP AS NON CORE | Summary: Genetic interaction with GID1A (Q9MAA7): gid1a gid1b double mutants show stronger fruit defects than gid1a alone. Reason: Experimentally supported but a downstream developmental output of GA perception, revealed only in combination with gid1a because of receptor redundancy. Supporting Evidence: PMID:24961590 Similarly to gid1a, gid1a gid1b had a proportional but stronger reduction in both silique length and seed number that resulted in a ratio similar to WT |
| GO:1905516 positive regulation of fertilization | IGI PMID:24961590 Role of the gibberellin receptors GID1 during fruit-set in A... | KEEP AS NON CORE | Summary: Genetic interaction with GID1A: gid1a gid1b plants have reduced seed set due to maternal (ovule) defects; GID1A and GID1B are the receptors expressed in ovules. Reason: Experimentally supported reproductive output of GA perception; downstream and redundant, not the molecular core function. Supporting Evidence: PMID:24961590 However, we found that the double mutant gid1a gid1b, which does not have GID1 activity in ovules, showed reduced seed-set even when fertilized by WT pollen |
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Download this section (compressed HTML)Q: Does GID1B bind DELLA proteins at physiologically meaningful levels in the absence of GA in planta, and does this GA-independent binding contribute to signaling in seeds?
Q: Is the narrow pH optimum of GID1B GA binding relevant to its function in ovules and imbibed seeds, where it is preferentially expressed?
Q: Why is GID1B not sufficient to sustain stem elongation in gid1a gid1c, given that its mRNA is detectable in stems: is the protein unstable there, or is it limited by DELLA preference?
Experiment: Compare GA-dependent and GA-independent GID1B-DELLA complex formation in imbibed seeds by co-immunoprecipitation in ga1-3 versus wild type, with GID1A as control.
Experiment: Swap the N-terminal lid region between GID1B and GID1A and test GA affinity, pH dependence and rescue of gid1a gid1c to map the determinants of GID1B-specific properties.
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