Gene Ontology annotation through association of InterPro records with GO terms
Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
Annotation inferences using phylogenetic trees
Electronic Gene Ontology annotations created by ARBA machine learning models
Identification and characterization of Arabidopsis gibberellin receptors.
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All three recombinant AtGID1 proteins bind bioactive gibberellins with highest affinity for GA4, and interact with DELLA proteins only in the presence of GA4 in yeast two-hybrid assays.
"The GA-binding activities of the three recombinant proteins were confirmed by an in vitro assay... all recombinants showed higher affinity to GA(4) than to other GAs."
Genetic characterization and functional analysis of the GID1 gibberellin receptors in Arabidopsis.
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GID1a-c are positive regulators of GA signaling; GA enhances GID1-DELLA interaction, and the GA-GID1 complex promotes DELLA-SLY1 interaction leading to DELLA degradation.
"the GA-GID1 complex promotes the interaction between RGA and the F-box protein SLY1, a component of the SCF(SLY1) E3 ubiquitin ligase that targets the DELLA protein for degradation"
The DELLA domain of GA INSENSITIVE mediates the interaction with the GA INSENSITIVE DWARF1A gibberellin receptor of Arabidopsis.
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The GAI DELLA domain is required and sufficient for GA-dependent interaction with the GID1A receptor, functioning as a receiver domain; gid1 triple mutants are GA insensitive.
"the GAI DELLA domain alone can mediate GA-dependent GID1A interactions, we propose that the DELLA domain functions as a receiver domain for activated GA receptors"
Multiple loss-of-function of Arabidopsis gibberellin receptor AtGID1s completely shuts down a gibberellin signal.
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The gid1a gid1b gid1c triple mutant is a severe dwarf that completely loses the ability to respond to applied GA, showing the GID1 receptors are required for GA signaling.
"the triple knockout seedlings completely lost their ability to respond to exogenously applied GA"
Global analysis of della direct targets in early gibberellin signaling in Arabidopsis.
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DELLA proteins feedback-regulate the expression of GA biosynthetic and GA receptor genes, placing GID1 receptor genes among GA-responsive genes.
"they help establish GA homeostasis by direct feedback regulation on the expression of GA biosynthetic and GA receptor genes"
Coordinated regulation of Arabidopsis thaliana development by light and gibberellins.
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GA-GID1-DELLA signaling intersects with light signaling; DELLA proteins block PIF3 and GA-induced DELLA degradation relieves this repression.
"DELLA proteins are GA-signalling repressors that block GA-induced development"
Proteolysis-independent downregulation of DELLA repression in Arabidopsis by the gibberellin receptor GIBBERELLIN INSENSITIVE DWARF1.
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GA-bound GID1 can inhibit DELLA repressor activity by direct interaction with the DELLA domain, independent of SLY1-mediated proteolysis.
"GA-bound GID1 can block DELLA repressor activity by direct protein-protein interaction with the DELLA domain. Thus, a SLY1-independent mechanism for GA signaling may function without DELLA degradation"
Gibberellin-induced DELLA recognition by the gibberellin receptor GID1.
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Crystal structure of the GID1A-GA-GAI(DELLA) ternary complex shows GID1A binds GA in a deep pocket capped by its N-terminal helical switch, which then binds the DELLA domain; GID1 is a nuclear receptor.
"GID1A occludes gibberellin in a deep binding pocket covered by its N-terminal helical switch region, which in turn interacts with the DELLA domain containing DELLA, VHYNP and LExLE motifs"
Differential expression and affinities of Arabidopsis gibberellin receptors can explain variation in phenotypes of multiple knock-out mutants.
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Differential expression and GID1-DELLA binding affinities among the three Arabidopsis GA receptors explain phenotypic variation among gid1 mutants.
"Differential expression and affinities of Arabidopsis gibberellin receptors can explain variation in phenotypes of multiple knock-out mutants"
Role of the gibberellin receptors GID1 during fruit-set in Arabidopsis.
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GID1A is the major GA receptor for fruit-set and pod growth, acts partially redundantly with GID1B/GID1C, and GID1 is a hormone-sensitive lipase-like protein WITHOUT hydrolase activity.
"GID1 was first described in rice as a nuclear localized protein similar to hormone-sensitive lipase family without hydrolase activity"
Tyrosine phosphorylation of the GARU E3 ubiquitin ligase promotes gibberellin signalling by preventing GID1 degradation.
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GID1 is a substrate of the RING E3 ligase GARU, which mediates ubiquitin-dependent degradation of GID1; GID1A localizes to the nucleus.
"GARU (GA receptor RING E3 ubiquitin ligase) mediates ubiquitin-dependent degradation of GID1"
Integrative Analysis from the Epigenome to Translatome Uncovers Patterns of Dominant Nuclear Regulation during Transient Stress.
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Genome-wide hypoxia/reoxygenation survey in which GID1A appears as one of many transcriptionally regulated genes (high-throughput expression pattern).
"we performed a survey spanning the epigenome to translatome of Arabidopsis (Arabidopsis thaliana) seedlings in response to hypoxia and reoxygenation"
Extensive signal integration by the phytohormone protein network.
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Large-scale yeast two-hybrid phytohormone interactome capturing GID1A protein-protein interactions including DELLAs and other partners.
"Extensive signal integration by the phytohormone protein network"
Falcon (Edison Scientific) deep research report for GID1A
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Synthesis of primary literature and reviews confirming GID1A is a soluble GA receptor with an esterase/lipase-like fold but no detectable hydrolase activity, binds bioactive GA (GA4 highest affinity), and triggers GA-dependent DELLA recognition leading to both proteolysis-dependent (SCF(SLY1)/ASK1) and proteolysis-independent suppression of DELLA; GID1A is nucleocytoplasmic.
"GID1A is the soluble GA receptor that binds bioactive GA and converts it into a protein–protein interaction signal by engaging DELLA motifs"
OpenScientist hypothesis adjudication: GID1A catalytic inactivity (broken HSL triad)
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Alignment against two active HSL-family enzymes (human AADAC and HSL) places their catalytic His at GID1A Val319, while Ser191, Asp289 and the HGG oxyanion motif are retained; residue identities confirmed against the UniProt sequence. This supports removing the InterPro-derived hydrolase activity annotation.
"GID1A retains the nucleophile Ser191 (in a GDSSG nucleophile elbow), the acid Asp289, and the HGG oxyanion loop (His113), but the general-base His is gone."
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The report states that no histidine nitrogen lies within catalytic distance of Ser191 in the AtGID1A crystal structure; this distance measurement was not independently re-run. The report's claims that GID1B/GID1C lack a gibberellin-binding annotation and that no hydrolase assay is published are respectively incorrect and overstated (see GID1A-notes.md).
"no histidine imidazole nitrogen within 8.5 Å of the Ser191 Oγ"