Evidence map›Paper›PMID 23832588›Full record

ArticleThe Plant cell2013

Trans-Golgi network localized ECHIDNA/Ypt interacting protein complex is required for the secretion of cell wall polysaccharides in Arabidopsis.

Delphine Gendre, Heather E McFarlane, Errin Johnson, Gregory Mouille, Andreas Sjödin, Jaesung Oh, Gabriel Levesque-Tremblay, Yoichiro Watanabe, Lacey Samuels, Rishikesh P Bhalerao

Open access · hybridAbstract 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 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
7.0field-weighted citation impact, top 2% 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

69 citing papers in PubMed, 127 citations in OpenAlex.

  1. Article
  2. Article
  3. Post-Golgi Trafficking in Plant Cells.Sub-cellular biochemistry · 2026
    Review
  4. Cargo Sorting Zones in Plant Trans-Golgi Network.Sub-cellular biochemistry · 2026
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. NKS1/ELMO4 is an integral protein of a pectin synthesis protein complex and maintains Golgi morphology and cell adhesion inProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Article
  15. The sorting of cargo proteins in the plantFrontiers in plant science · 2022
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

9 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

10 authors at 4 institutions in 3 countries.

Delphine GendreUmeå Plant Science Centre, Department of Forest Genetics and Plant Physiology, Swedish University of Agricultural Sciences, S-901 83 Umea, Sweden.
Heather E McFarlane
Errin Johnson
Gregory Mouille
Andreas Sjödin
Jaesung Oh
Gabriel Levesque-Tremblay
Yoichiro Watanabe
Lacey Samuels
Rishikesh P Bhalerao
University of British Columbia · CASwedish University of Agricultural Sciences · SEUmeå Plant Science Centre · SEInstitut Jean-Pierre Bourgin · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The secretion of cell wall polysaccharides through the trans-Golgi network (TGN) is required for plant cell elongation. However, the components mediating the post-Golgi secretion of pectin and hemicellulose, the two major cell wall polysaccharides, are largely unknown. We identified evolutionarily conserved YPT/RAB GTPase Interacting Protein 4a (YIP4a) and YIP4b (formerly YIP2), which form a TGN-localized complex with ECHIDNA (ECH) in Arabidopsis thaliana. The localization of YIP4 and ECH proteins at the TGN is interdependent and influences the localization of VHA-a1 and SYP61, which are key components of the TGN. YIP4a and YIP4b act redundantly, and the yip4a yip4b double mutants have a cell elongation defect. Genetic, biochemical, and cell biological analyses demonstrate that the ECH/YIP4 complex plays a key role in TGN-mediated secretion of pectin and hemicellulose to the cell wall in dark-grown hypocotyls and in secretory cells of the seed coat. In keeping with these observations, Fourier transform infrared microspectroscopy analysis revealed that the ech and yip4a yip4b mutants exhibit changes in their cell wall composition. Overall, our results reveal a TGN subdomain defined by ECH/YIP4 that is required for the secretion of pectin and hemicellulose and distinguishes the role of the TGN in secretion from its roles in endocytic and vacuolar trafficking.

Indexed as

Amino Acid SequenceArabidopsisArabidopsis ProteinsCell WallLuminescent ProteinsMicroscopy, ConfocalMolecular Sequence DataMultiprotein ComplexesMutationPhylogenyPlants, Genetically ModifiedPolysaccharidesProtein BindingSequence Homology, Amino Acidtrans-Golgi NetworkTwo-Hybrid System TechniquesArabidopsis ProteinsLuminescent ProteinsMultiprotein ComplexesPolysaccharides

Identifiers

PMID23832588
PMCPMC3753388
OpenAlexW2120780367

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.