Evidence map›Paper›PMID 11717468›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2001

The DELLA motif is essential for gibberellin-induced degradation of RGA.

A Dill, H S Jung, T P Sun

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 197 papers.

0numbers the graph read from it
0cells of the map it votes in
197citing papers in PubMed
29.2field-weighted citation impact, top 1% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

197 citing papers in PubMed, 478 citations in OpenAlex.

  1. CDK8 phosphorylation of DELLA limits Mediator recruitment in gibberellin signaling.Proceedings of the National Academy of Sciences of the United States of America · 2026
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  7. Review
  8. Genome-wide analysis of theFrontiers in plant science · 2026
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  10. A mutation of GRAS SCL14 gene confers moderate sensitivity to the herbicide bentazon in soybean.TAG. Theoretical and applied genetics. Theoretische und angewandte Genetik · 2025
    Article
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  15. Article
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  17. Review
  18. Gibberellic Acid (GAChemistry & biodiversity · 2025
    Review
  19. Article
  20. Review

137 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

3 authors at 2 institutions in 1 country.

A DillDepartment of Biology, Duke University, Durham, NC 27708, USA.
H S Jung
T P Sun
Duke University · USMichigan State University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

RGA and GAI are homologous genes that encode putative transcriptional regulators that repress gibberellin (GA) signaling in Arabidopsis. Previously we showed that the green fluorescent protein (GFP)-RGA fusion protein is localized to the nucleus in transgenic Arabidopsis, and expression of this fusion protein rescues the rga null mutation. The GA signal seems to derepress the GA response pathway by degrading the repressor protein RGA. The GA-insensitive, semidominant, semidwarf gai-1 mutant encodes a mutant protein with a 17-amino acid deletion within the DELLA domain of GAI. It was hypothesized that this mutation turns the gai protein into a constitutive repressor of GA signaling. Because the sequences missing in gai-1 are identical between GAI and RGA, we tested whether an identical mutation (rga-Delta 17) in the RGA gene would confer a phenotype similar to gai-1. We demonstrated that expression of rga-Delta 17 or GFP-(rga-Delta 17) under the control of the RGA promoter caused a GA-unresponsive severe dwarf phenotype in transgenic Arabidopsis. Analysis of the mRNA levels of a GA biosynthetic gene, GA4, showed that the feedback control of GA biosynthesis in these transgenic plants was less responsive to GA than that in wild type. Immunoblot and confocal microscopy analyses indicated that rga-Delta17 and GFP-(rga-Delta 17) proteins were resistant to degradation after GA application. Our results illustrate that the DELLA domain in RGA plays a regulatory role in GA-induced degradation of RGA. Deletion of this region stabilizes the rga-Delta 17 mutant protein, and regardless of the endogenous GA status rga-Delta 17 becomes a constitutively active repressor of GA signaling.

Indexed as

Amino Acid MotifsArabidopsisGene ExpressionGibberellinsGreen Fluorescent ProteinsLuminescent ProteinsPlant ProteinsPlants, Genetically ModifiedRecombinant Fusion ProteinsStructure-Activity RelationshipTranscription FactorsGibberellinsGreen Fluorescent ProteinsLuminescent ProteinsPlant ProteinsRecombinant Fusion ProteinsTranscription Factors

Identifiers

PMID11717468
PMCPMC61185
OpenAlexW2078453895

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.