Evidence map›Paper›PMID 30464344›Full record

ArticleNature2018

Structural plasticity of D3-D14 ubiquitin ligase in strigolactone signalling.

Nitzan Shabek, Fabrizio Ticchiarelli, Haibin Mao, Thomas R Hinds, Ottoline Leyser, Ning Zheng

Open access · greenAbstract read
In one paragraph

Article in Nature, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 96 papers.

0numbers the graph read from it
0cells of the map it votes in
96citing papers in PubMed
26.4field-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

96 citing papers in PubMed, 199 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. TED1 Promotes the Assembly of SCFAdvanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
    Article
  5. Article
  6. Towards an integrated molecular understanding of plant hormones.Journal of integrative plant biology · 2026
    Review
  7. Review
  8. Review
  9. Article
  10. Review
  11. Localized heme sensing through a ternary molecular glue.bioRxiv : the preprint server for biology · 2026
    Article
  12. Article
  13. Article
  14. Article
  15. Mapping Strigolactone Hydrolysis in DWARF14 via QM/MM String Method.bioRxiv : the preprint server for biology · 2026
    Article
  16. Molecular insights into volatile organic compound sensing and signaling in plants.The Plant journal : for cell and molecular biology · 2026
    Review
  17. Article
  18. Unusually broad-spectrum small-molecule sensing using a single protein scaffold.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  19. Article
  20. Article

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

6 authors at 3 institutions in 2 countries.

Nitzan ShabekDepartment of Pharmacology, University of Washington, Seattle, WA, USA.
Fabrizio TicchiarelliThe Sainsbury Laboratory, University of Cambridge, Cambridge, UK.
Haibin MaoDepartment of Pharmacology, University of Washington, Seattle, WA, USA.
Thomas R HindsDepartment of Pharmacology, University of Washington, Seattle, WA, USA.
Ottoline LeyserThe Sainsbury Laboratory, University of Cambridge, Cambridge, UK.
Ning ZhengDepartment of Pharmacology, University of Washington, Seattle, WA, USA. nzheng@uw.edu.
University of Washington · USUniversity of Cambridge · GBUniversity of California, Davis · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

The strigolactones, a class of plant hormones, regulate many aspects of plant physiology. In the inhibition of shoot branching, the α/β hydrolase D14-which metabolizes strigolactone-interacts with the F-box protein D3 to ubiquitinate and degrade the transcription repressor D53. Despite the fact that multiple modes of interaction between D14 and strigolactone have recently been determined, how the hydrolase functions with D3 to mediate hormone-dependent D53 ubiquitination remains unknown. Here we show that D3 has a C-terminal α-helix that can switch between two conformational states. The engaged form of this α-helix facilitates the binding of D3 and D14 with a hydrolysed strigolactone intermediate, whereas the dislodged form can recognize unmodified D14 in an open conformation and inhibits its enzymatic activity. The D3 C-terminal α-helix enables D14 to recruit D53 in a strigolactone-dependent manner, which in turn activates the hydrolase. By revealing the structural plasticity of the SCF

Indexed as

Signal TransductionHeterocyclic Compounds, 3-RingLactonesModels, MolecularMultienzyme ComplexesOryzaPlant Growth RegulatorsPlant ProteinsProtein BindingProtein Structure, SecondarySKP Cullin F-Box Protein LigasesStructure-Activity RelationshipUbiquitinUbiquitinationGR24 strigolactoneHeterocyclic Compounds, 3-RingLactonesMultienzyme ComplexesPlant Growth RegulatorsPlant ProteinsSKP Cullin F-Box Protein LigasesUbiquitin

Identifiers

PMID30464344
PMCPMC6265067
OpenAlexW2901661105

What OpenQuestion holds

Textmetadata
LicenceTDM
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.