Evidence map›Paper›PMID 23543785›Full record

ArticleThe Plant cell2013

Roles of N-terminal fatty acid acylations in membrane compartment partitioning: Arabidopsis h-type thioredoxins as a case study.

José A Traverso, Chiara Micalella, Aude Martinez, Spencer C Brown, Béatrice Satiat-Jeunemaître, Thierry Meinnel, Carmela Giglione

Open access · bronzeAbstract 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 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
3.4field-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

21 citing papers in PubMed, 79 citations in OpenAlex.

  1. Arabidopsis proteinProceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  2. Members of theInternational journal of molecular sciences · 2024
    Article
  3. Review
  4. Article
  5. Article
  6. ThioredoxinAntioxidants (Basel, Switzerland) · 2021
    Article
  7. Protein Phosphorylation Response to Abiotic Stress in Plants.Methods in molecular biology (Clifton, N.J.) · 2021
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Targeted Profiling ofThe Plant cell · 2018
    Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review
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

7 authors at 2 institutions in 2 countries.

José A TraversoCentre National de la Recherche Scientifique, Centre de Recherche de Gif, Institut des Sciences du Végétal, F-91198 Gif-sur-Yvette cedex, France.
Chiara Micalella
Aude Martinez
Spencer C Brown
Béatrice Satiat-Jeunemaître
Thierry Meinnel
Carmela Giglione
Institut des Sciences du Végétal · FRConsejo Superior de Investigaciones Científicas · ES

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

N-terminal fatty acylations (N-myristoylation [MYR] and S-palmitoylation [PAL]) are crucial modifications affecting 2 to 4% of eukaryotic proteins. The role of these modifications is to target proteins to membranes. Predictive tools have revealed unexpected targets of these acylations in Arabidopsis thaliana and other plants. However, little is known about how N-terminal lipidation governs membrane compartmentalization of proteins in plants. We show here that h-type thioredoxins (h-TRXs) cluster in four evolutionary subgroups displaying strictly conserved N-terminal modifications. It was predicted that one subgroup undergoes only MYR and another undergoes both MYR and PAL. We used plant TRXs as a model protein family to explore the effect of MYR alone or MYR and PAL in the same family of proteins. We used a high-throughput biochemical strategy to assess MYR of specific TRXs. Moreover, various TRX-green fluorescent protein fusions revealed that MYR localized protein to the endomembrane system and that partitioning between this membrane compartment and the cytosol correlated with the catalytic efficiency of the N-myristoyltransferase acting at the N terminus of the TRXs. Generalization of these results was obtained using several randomly selected Arabidopsis proteins displaying a MYR site only. Finally, we demonstrated that a palmitoylatable Cys residue flanking the MYR site is crucial to localize proteins to micropatching zones of the plasma membrane.

Indexed as

AcylationAmino Acid SequenceArabidopsisBinding SitesCell MembraneCysteineCytosolEndoplasmic ReticulumEnzyme ActivationFatty AcidsFluorescence Recovery After PhotobleachingGreen Fluorescent ProteinsMembrane LipidsPhylogenyProtein TransportThioredoxin hCysteineFatty AcidsGreen Fluorescent ProteinsMembrane LipidsThioredoxin h

Identifiers

PMID23543785
PMCPMC3634677
OpenAlexW2161480259

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.