Evidence map›Paper›PMID 23572542›Full record

ArticleThe Plant cell2013

Arabidopsis Sec1/Munc18 protein SEC11 is a competitive and dynamic modulator of SNARE binding and SYP121-dependent vesicle traffic.

Rucha Karnik, Christopher Grefen, Robert Bayne, Annegret Honsbein, Tim Köhler, Dimitrios Kioumourtzoglou, Mary Williams, Nia J Bryant, Michael R Blatt

Abstract read
In one paragraph

Article in The Plant cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.

0numbers the graph read from it
0cells of the map it votes in
53citing papers in PubMed
–field-weighted citation impact
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

53 citing papers in PubMed.

  1. Review
  2. Article
  3. COJournal of integrative plant biology · 2026
    Article
  4. Article
  5. GORK KNature communications · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Roles of the ArabidopsisInternational journal of molecular sciences · 2024
    Article
  11. Article
  12. Engineering a KNature plants · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article
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

9 authors.

Rucha KarnikLaboratory of Plant Physiology and Biophysics, University of Glasgow, Glasgow G12 8QQ, United Kingdom.
Christopher Grefen
Robert Bayne
Annegret Honsbein
Tim Köhler
Dimitrios Kioumourtzoglou
Mary Williams
Nia J Bryant
Michael R Blatt

Funding

Biotechnology and Biological Sciences Research Council BB/E024904/1Biotechnology and Biological Sciences Research Council BB/F001630/1Biotechnology and Biological Sciences Research Council BB/F001673/1Biotechnology and Biological Sciences Research Council BB/H009817/1Biotechnology and Biological Sciences Research Council BB/H024867/1Biotechnology and Biological Sciences Research Council P12750
6 · The paper itself

Abstract

The Arabidopsis thaliana Qa-SNARE SYP121 (=SYR1/PEN1) drives vesicle traffic at the plasma membrane of cells throughout the vegetative plant. It facilitates responses to drought, to the water stress hormone abscisic acid, and to pathogen attack, and it is essential for recovery from so-called programmed stomatal closure. How SYP121-mediated traffic is regulated is largely unknown, although it is thought to depend on formation of a fusion-competent SNARE core complex with the cognate partners VAMP721 and SNAP33. Like SYP121, the Arabidopsis Sec1/Munc18 protein SEC11 (=KEULE) is expressed throughout the vegetative plant. We find that SEC11 binds directly with SYP121 both in vitro and in vivo to affect secretory traffic. Binding occurs through two distinct modes, one requiring only SEC11 and SYP121 and the second dependent on assembly of a complex with VAMP721 and SNAP33. SEC11 competes dynamically for SYP121 binding with SNAP33 and VAMP721, and this competition is predicated by SEC11 association with the N terminus of SYP121. These and additional data are consistent with a model in which SYP121-mediated vesicle fusion is regulated by an unusual "handshaking" mechanism of concerted SEC11 debinding and rebinding. They also implicate one or more factors that alter or disrupt SEC11 association with the SYP121 N terminus as an early step initiating SNARE complex formation.

Indexed as

ArabidopsisArabidopsis ProteinsBinding, CompetitiveCarrier ProteinsCell Cycle ProteinsCell MembraneImmunoblottingLuminescent ProteinsMicroscopy, ConfocalMutationPlants, Genetically ModifiedProtein BindingQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsR-SNARE ProteinsArabidopsis ProteinsAT1G12360 protein, ArabidopsisCarrier ProteinsCell Cycle ProteinsLuminescent ProteinsPEN1 protein, ArabidopsisQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsR-SNARE ProteinsSNAP33 protein, ArabidopsisVAMP721 protein, Arabidopsis

Identifiers

PMID23572542
PMCPMC3663274

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.