Evidence map›Paper›PMID 26470846›Full record

ArticleCell research2015

Destabilization of strigolactone receptor DWARF14 by binding of ligand and E3-ligase signaling effector DWARF3.

Li-Hua Zhao, X Edward Zhou, Wei Yi, Zhongshan Wu, Yue Liu, Yanyong Kang, Li Hou, Parker W de Waal, Suling Li, Yi Jiang and 9 more

Open access · greenAbstract read
In one paragraph

Article in Cell research, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 86 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
86citing papers in PubMed, 1 pooled it
31.0field-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

86 citing papers in PubMed, 1 synthesis or guideline pooled it, 180 citations in OpenAlex.

  1. Pooled it
  2. Negative feedback regulation of karrikin signaling inProceedings of the National Academy of Sciences of the United States of America · 2026
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  3. TED1 Promotes the Assembly of SCFAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  4. Towards an integrated molecular understanding of plant hormones.Journal of integrative plant biology · 2026
    Review
  5. Article
  6. Structure-informed engineering of plant-microbe interactions.The Plant journal : for cell and molecular biology · 2026
    Review
  7. Mapping Strigolactone Hydrolysis in DWARF14 via QM/MM String Method.bioRxiv : the preprint server for biology · 2026
    Article
  8. Article
  9. Article
  10. Article
  11. Review
  12. Article
  13. Structural requirements of KAI2 ligands for activation of signal transduction.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Article
  17. International journal of molecular sciences · 2024
    Article
  18. Article
  19. Article
  20. Article

26 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

19 authors at 7 institutions in 3 countries.

Li-Hua ZhaoVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
X Edward ZhouLaboratory of Structural Sciences and Laboratory of Structural Biology and Biochemistry, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Wei YiVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Zhongshan WuVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Yue LiuVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Yanyong KangLaboratory of Structural Sciences and Laboratory of Structural Biology and Biochemistry, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Li HouVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Parker W de WaalLaboratory of Structural Sciences and Laboratory of Structural Biology and Biochemistry, Van Andel Research Institute, Grand Rapids, Michigan, USA.
Suling LiVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Yi JiangVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Adrian ScaffidiSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, WA 6009, Australia.
Gavin R FlemattiSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, WA 6009, Australia.
Steven M SmithSchool of Chemistry and Biochemistry, The University of Western Australia, Crawley, WA 6009, Australia.
Vinh Q LamDepartment of Molecular Therapeutics, Translational Research Institute, The Scripps Research Institute, Scripps Florida, Jupiter, FL 33458, USA.
Patrick R GriffinDepartment of Molecular Therapeutics, Translational Research Institute, The Scripps Research Institute, Scripps Florida, Jupiter, FL 33458, USA.
Yonghong WangState Key Laboratory of Plant Genomics and National Center for Plant Gene Research (Beijing), Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Jiayang LiState Key Laboratory of Plant Genomics and National Center for Plant Gene Research (Beijing), Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing 100101, China.
Karsten MelcherVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
H Eric XuVARI-SIMM Center, Center for Structure and Function of Drug Targets, Key Laboratory of Receptor Research, Shanghai Institute of Materia Medica, Chinese Academy of Sciences, Shanghai 201203, China.
Chinese Academy of Sciences · CNShanghai Institute of Materia Medica · CNVan Andel Institute · USInstitute of Genetics and Developmental Biology · CNScripps Research Institute · USUniversity of Western Australia · AUState Key Laboratory of Plant Genomics · CN

Funding

Structural Genomics of Orphan Nuclear ReceptorsR01DK071662 · NIDDK · VAN ANDEL RESEARCH INSTITUTE · PI XU, H ERIC · 2005 to 2017
$5.1M
Structural interrogation of allosteric AMPK regulationR01GM104212 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2013 to 2016
$1.5M
Structural and functional analysis of a dynamic ABA signaling complexR01GM102545 · NIGMS · VAN ANDEL RESEARCH INSTITUTE · PI MELCHER, KARSTEN · 2012 to 2014
$1.1M
NIDDK NIH HHS DK071662NIDDK NIH HHS R01 DK071662NIGMS NIH HHS GM102545NIGMS NIH HHS GM104212NIGMS NIH HHS R01 GM102545NIGMS NIH HHS R01 GM104212
6 · The paper itself

Abstract

Strigolactones (SLs) are endogenous hormones and exuded signaling molecules in plant responses to low levels of mineral nutrients. Key mediators of the SL signaling pathway in rice include the α/β-fold hydrolase DWARF 14 (D14) and the F-box component DWARF 3 (D3) of the ubiquitin ligase SCF(D3) that mediate ligand-dependent degradation of downstream signaling repressors. One perplexing feature is that D14 not only functions as the SL receptor but is also an active enzyme that slowly hydrolyzes diverse natural and synthetic SLs including GR24, preventing the crystallization of a binary complex of D14 with an intact SL as well as the ternary D14/SL/D3 complex. Here we overcome these barriers to derive a structural model of D14 bound to intact GR24 and identify the interface that is required for GR24-mediated D14-D3 interaction. The mode of GR24-mediated signaling, including ligand recognition, hydrolysis by D14, and ligand-mediated D14-D3 interaction, is conserved in structurally diverse SLs. More importantly, D14 is destabilized upon the binding of ligands and D3, thus revealing an unusual mechanism of SL recognition and signaling, in which the hormone, the receptor, and the downstream effectors are systematically destabilized during the signal transduction process.

Indexed as

Signal TransductionHeterocyclic Compounds, 3-RingLactonesOryzaPlant Growth RegulatorsPlant ProteinsSKP Cullin F-Box Protein LigasesGR24 strigolactoneHeterocyclic Compounds, 3-RingLactonesPlant Growth RegulatorsPlant ProteinsSKP Cullin F-Box Protein Ligases

Identifiers

PMID26470846
PMCPMC4650425
OpenAlexW2197423430

What OpenQuestion holds

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Registered trials

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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.