Evidence map›Paper›PMID 10810147›Full record

ArticleThe Plant cell2000

Protein recycling from the Golgi apparatus to the endoplasmic reticulum in plants and its minor contribution to calreticulin retention.

S Pagny, M Cabanes-Macheteau, J W Gillikin, N Leborgne-Castel, P Lerouge, R S Boston, L Faye, V Gomord

Open access · bronzeAbstract read
In one paragraph

Article in The Plant cell, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.2field-weighted citation impact, top 8% 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

48 citing papers in PubMed, 108 citations in OpenAlex.

  1. Article
  2. Plants (Basel, Switzerland) · 2021
    Article
  3. Article
  4. ComplexFrontiers in plant science · 2021
    Article
  5. Article
  6. Article
  7. Article
  8. Secretory Phospholipases AFrontiers in plant science · 2019
    Review
  9. Article
  10. Article
  11. Plant protein glycosylation.Glycobiology · 2016
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Expression of recombinant vaccines and antibodies in plants.Monoclonal antibodies in immunodiagnosis and immunotherapy · 2014
    Review
  17. Article
  18. Article
  19. Article
  20. Evolutionarily conserved glycan signal to degrade aberrant brassinosteroid receptors in Arabidopsis.Proceedings of the National Academy of Sciences of the United States of America · 2012
    Article
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

8 authors at 3 institutions in 2 countries.

S PagnyLaboratoire des Transports Intracellulaires, CNRS-ESA 6037, IFRMP23, Université de Rouen, 76821 Mont St. Aignan Cedex, France.
M Cabanes-Macheteau
J W Gillikin
N Leborgne-Castel
P Lerouge
R S Boston
L Faye
V Gomord
Université de Rouen Normandie · FRNorth Carolina State University · USCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Using pulse-chase experiments combined with immunoprecipitation and N-glycan structural analysis, we showed that the retrieval mechanism of proteins from post-endoplasmic reticulum (post-ER) compartments is active in plant cells at levels similar to those described previously for animal cells. For instance, recycling from the Golgi apparatus back to the ER is sufficient to block the secretion of as much as 90% of an extracellular protein such as the cell wall invertase fused with an HDEL C-terminal tetrapeptide. Likewise, recycling can sustain fast retrograde transport of Golgi enzymes into the ER in the presence of brefeldin A. However, on the basis of our data, we propose that this retrieval mechanism in plants has little impact on the ER retention of a soluble ER protein such as calreticulin. Indeed, the latter is retained in the ER without any N-glycan-related evidence for a recycling through the Golgi apparatus. Taken together, these results indicate that calreticulin and perhaps other plant reticuloplasmins are possibly largely excluded from vesicles exported from the ER. Instead, they are probably retained in the ER by mechanisms that rely primarily on signals other than H/KDEL motifs.

Indexed as

Base Sequencebeta-FructofuranosidaseBrefeldin ACalcium-Binding ProteinsCalreticulinDNA PrimersEndoplasmic ReticulumGlycoside HydrolasesGolgi ApparatusHydrolysisMannosePlant ProteinsPolysaccharidesProtein Processing, Post-TranslationalRibonucleoproteinsZea maysbeta-FructofuranosidaseBrefeldin ACalcium-Binding ProteinsCalreticulinDNA PrimersGlycoside HydrolasesMannosePlant ProteinsPolysaccharidesRibonucleoproteins

Identifiers

PMID10810147
PMCPMC139924
OpenAlexW2156437132

What OpenQuestion holds

Textmetadata
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.