Evidence map›Paper›PMID 20729862›Full record

ArticleNature structural & molecular biology2010

Identification and mechanism of ABA receptor antagonism.

Karsten Melcher, Yong Xu, Ley-Moy Ng, X Edward Zhou, Fen-Fen Soon, Viswanathan Chinnusamy, Kelly M Suino-Powell, Amanda Kovach, Fook S Tham, Sean R Cutler and 4 more

Open access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
24.4field-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

68 citing papers in PubMed, 159 citations in OpenAlex.

  1. PHLPP is neither a Phosphatase nor a Tumor Suppressor.BioEssays : news and reviews in molecular, cellular and developmental biology · 2026
    Review
  2. Evolutionary-based remodeling of ABA receptors reveals the structural basis of hormone perception and regulation.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Label-Free Quantitative Proteomics Reveal the Involvement of PRT6 inInternational journal of molecular sciences · 2022
    Article
  9. Plants (Basel, Switzerland) · 2022
    Article
  10. Review
  11. Article
  12. Article
  13. An Update on Crop ABA Receptors.Plants (Basel, Switzerland) · 2021
    Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

14 authors at 5 institutions in 3 countries.

Karsten MelcherLaboratory of Structural Sciences, Van Andel Research Institute, Grand Rapids, Michigan, USA. Karsten.Melcher@vai.org
Yong Xu
Ley-Moy Ng
X Edward Zhou
Fen-Fen Soon
Viswanathan Chinnusamy
Kelly M Suino-Powell
Amanda Kovach
Fook S Tham
Sean R Cutler
Jun Li
Eu-Leong Yong
Jian-Kang Zhu
H Eric Xu
Van Andel Institute · USKing Abdullah University of Science and Technology · SANational University of Singapore · SGUniversity of California, Riverside · USNational University Hospital · SG

Funding

Structural Genomics of Orphan Nuclear ReceptorsR01DK071662 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2005 to 2017
$5.1M
CALCIUM SIGNALING--INTRACELL ION HOMEOSTASIS REGULATIONR01GM059138 · NIGMS · UNIVERSITY OF CALIFORNIA RIVERSIDE · PI ZHU, JIAN-KANG · 1999 to 2015
$4.4M
Structure and Functions of Steroid Hormone ReceptorsR01DK066202 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2006 to 2010
$2.0M
Structural and functional studies of the nuclear receptor PPARgammaR01HL089301 · NHLBI · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2007 to 2010
$1.8M
Structural Biology of Class B G-Protein Coupled ReceptorsR01GM087413 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2009 to 2010
$764k
NHLBI NIH HHS R01 HL089301NIDDK NIH HHS R01 DK066202NIDDK NIH HHS R01 DK071662NIGMS NIH HHS R01 GM059138NIGMS NIH HHS R01 GM087413
6 · The paper itself

Abstract

The phytohormone abscisic acid (ABA) functions through a family of fourteen PYR/PYL receptors, which were identified by resistance to pyrabactin, a synthetic inhibitor of seed germination. ABA activates these receptors to inhibit type 2C protein phosphatases, such as ABI1, yet it remains unclear whether these receptors can be antagonized. Here we demonstrate that pyrabactin is an agonist of PYR1 and PYL1 but is unexpectedly an antagonist of PYL2. Crystal structures of the PYL2-pyrabactin and PYL1-pyrabactin-ABI1 complexes reveal the mechanism responsible for receptor-selective activation and inhibition, which enables us to design mutations that convert PYL1 to a pyrabactin-inhibited receptor and PYL2 to a pyrabactin-activated receptor and to identify new pyrabactin-based ABA receptor agonists. Together, our results establish a new concept of ABA receptor antagonism, illustrate its underlying mechanisms and provide a rational framework for discovering novel ABA receptor ligands.

Indexed as

Abscisic AcidArabidopsisArabidopsis ProteinsCrystallography, X-RayMembrane Transport ProteinsModels, MolecularNaphthalenesProtein Interaction Domains and MotifsProtein Structure, QuaternarySulfonamidesAbscisic AcidArabidopsis ProteinsAT4G17870 protein, ArabidopsisMembrane Transport ProteinsNaphthalenespyrabactinSulfonamides

Identifiers

PMID20729862
PMCPMC2933329
OpenAlexW2026011395

What OpenQuestion holds

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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.