Evidence map›Paper›PMID 37188854›Full record

ArticleNature plants2023

Structure and sucrose binding mechanism of the plant SUC1 sucrose transporter.

Laust Bavnhøj, Jan Heiner Driller, Lorena Zuzic, Amanda Dyrholm Stange, Birgit Schiøtt, Bjørn Panyella Pedersen

Open access · hybridAbstract read
In one paragraph

Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
17.1field-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

23 citing papers in PubMed, 43 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Structural basis of glucose-6-phosphate transport by human SLC37A2.Nature structural & molecular biology · 2026
    Article
  8. Article
  9. Article
  10. Review
  11. Review
  12. Article
  13. Article
  14. Comparative analysis of STP6 and STP10 unravels molecular selectivity in sugar transport proteins.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  15. Key sugar transporters drive development and pathogenicity inFrontiers in cellular and infection microbiology · 2025
    Article
  16. From Division to Death: Metabolomic Analysis ofPlants (Basel, Switzerland) · 2024
    Article
  17. Review
  18. Article
  19. Review
  20. Plant Heterotrophic Cultures: No Food, No Growth.Plants (Basel, Switzerland) · 2024
    Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

6 authors at 1 institution in 1 country.

Laust BavnhøjDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.
Jan Heiner DrillerDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark.ORCID http://orcid.org/0000-0001-7561-964X
Lorena ZuzicDepartment of Chemistry, Aarhus University, Aarhus, Denmark.ORCID http://orcid.org/0000-0002-7834-612X
Amanda Dyrholm StangeDepartment of Chemistry, Aarhus University, Aarhus, Denmark.ORCID http://orcid.org/0000-0001-9090-211X
Birgit SchiøttDepartment of Chemistry, Aarhus University, Aarhus, Denmark.ORCID http://orcid.org/0000-0001-9937-1562
Bjørn Panyella PedersenDepartment of Molecular Biology and Genetics, Aarhus University, Aarhus, Denmark. bpp@mbg.au.dk.ORCID http://orcid.org/0000-0001-7860-7230
Aarhus University · DK

Funding

EC | EU Framework Programme for Research and Innovation H2020 | H2020 Priority Excellent Science | H2020 European Research Council (H2020 Excellent Science - European Research Council) 101000936Lundbeckfonden (Lundbeck Foundation) R346-2020-1944Novo Nordisk Fonden (Novo Nordisk Foundation) NF20OC0065431Novo Nordisk Fonden (Novo Nordisk Foundation) NNF18OC0032608
6 · The paper itself

Abstract

Sucrose import from photosynthetic tissues into the phloem is mediated by transporters from the low-affinity sucrose transporter family (SUC/SUT family). Furthermore, sucrose redistribution to other tissues is driven by phloem sap movement, the product of high turgor pressure created by this import activity. Additionally, sink organs such as fruits, cereals and seeds that accumulate high concentrations of sugar also depend on this active transport of sucrose. Here we present the structure of the sucrose-proton symporter, Arabidopsis thaliana SUC1, in an outward open conformation at 2.7 Å resolution, together with molecular dynamics simulations and biochemical characterization. We identify the key acidic residue required for proton-driven sucrose uptake and describe how protonation and sucrose binding are strongly coupled. Sucrose binding is a two-step process, with initial recognition mediated by the glucosyl moiety binding directly to the key acidic residue in a stringent pH-dependent manner. Our results explain how low-affinity sucrose transport is achieved in plants, and pinpoint a range of SUC binders that help define selectivity. Our data demonstrate a new mode for proton-driven symport with links to cation-driven symport and provide a broad model for general low-affinity transport in highly enriched substrate environments.

Indexed as

ArabidopsisSucroseBiological TransportMembrane Transport ProteinsPlant ProteinsProtonsMembrane Transport ProteinsPlant ProteinsProtonsSucrose

Identifiers

PMID37188854
PMCPMC10281868
OpenAlexW4376609071

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.