Evidence map›Paper›PMID 24563205›Full record

ArticleThe Plant cell2014

Targeted degradation of abscisic acid receptors is mediated by the ubiquitin ligase substrate adaptor DDA1 in Arabidopsis.

María Luisa Irigoyen, Elisa Iniesto, Lesia Rodriguez, María Isabel Puga, Yuki Yanagawa, Elah Pick, Elizabeth Strickland, Javier Paz-Ares, Ning Wei, Geert De Jaeger and 3 more

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 96 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed, 1 pooled it
28.0field-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

96 citing papers in PubMed, 1 synthesis or guideline pooled it, 194 citations in OpenAlex.

  1. Pooled it
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  11. Identification ofForestry research · 2025
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  15. Identification and Expression Analysis of theInternational journal of molecular sciences · 2023
    Article
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36 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

13 authors at 3 institutions in 3 countries.

María Luisa IrigoyenCentro Nacional de Biotecnología-Consejo Superior de Investigaciones Científicas, 28049 Madrid, Spain.
Elisa Iniesto
Lesia Rodriguez
María Isabel Puga
Yuki Yanagawa
Elah Pick
Elizabeth Strickland
Javier Paz-Ares
Ning Wei
Geert De Jaeger
Pedro L Rodriguez
Xing Wang Deng
Vicente Rubio
Consejo Superior de Investigaciones Científicas · ESYale University · USGhent University · BE

Funding

Analysis of a Light-Regulated Development SwitchR37GM047850 · NIGMS · YALE UNIVERSITY · PI DENG, XING WANG · 2004 to 2013
$5.7M
LIGHT SIGNAL TRANDUCTION IN ARABIDOPSISR01GM047850 · NIGMS · YALE UNIVERSITY · PI WEI, NING · 1996 to 2018
$4.1M
LIGHT SIGNAL TRANSDUCTION IN ARABIDOPSISR29GM047850 · NIGMS · YALE UNIVERSITY · PI DENG, XING WANG · 1992 to 1995
–
NIGMS NIH HHS GM-47850NIGMS NIH HHS R01 GM047850NIGMS NIH HHS R37 GM047850
6 · The paper itself

Abstract

CULLIN4-RING E3 ubiquitin ligases (CRL4s) regulate key developmental and stress responses in eukaryotes. Studies in both animals and plants have led to the identification of many CRL4 targets as well as specific regulatory mechanisms that modulate their function. The latter involve COP10-DET1-DDB1 (CDD)-related complexes, which have been proposed to facilitate target recognition by CRL4, although the molecular basis for this activity remains largely unknown. Here, we provide evidence that Arabidopsis thaliana DET1-, DDB1-ASSOCIATED1 (DDA1), as part of the CDD complex, provides substrate specificity for CRL4 by interacting with ubiquitination targets. Thus, we show that DDA1 binds to the abscisic acid (ABA) receptor PYL8, as well as PYL4 and PYL9, in vivo and facilitates its proteasomal degradation. Accordingly, we found that DDA1 negatively regulates ABA-mediated developmental responses, including inhibition of seed germination, seedling establishment, and root growth. All other CDD components displayed a similar regulatory function, although they did not directly interact with PYL8. Interestingly, DDA1-mediated destabilization of PYL8 is counteracted by ABA, which protects PYL8 by limiting its polyubiquitination. Altogether, our data establish a function for DDA1 as a substrate receptor for CRL4-CDD complexes and uncover a mechanism for the desensitization of ABA signaling based on the regulation of ABA receptor stability.

Indexed as

ProteolysisAbscisic AcidArabidopsisArabidopsis ProteinsModels, BiologicalMultiprotein ComplexesMutationPolyubiquitinProteasome Endopeptidase ComplexProtein BindingReceptors, Cell SurfaceSaccharomyces cerevisiaeSubstrate SpecificityUbiquitinationUbiquitin-Protein LigasesAbscisic AcidArabidopsis ProteinsDDA1 (DDB1-ASSOCIATED1) protein, ArabidopsisMultiprotein ComplexesPolyubiquitinProteasome Endopeptidase ComplexReceptors, Cell SurfaceUbiquitin-Protein Ligases

Identifiers

PMID24563205
PMCPMC3967035
OpenAlexW2107345958

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.