Evidence map›Paper›PMID 21697507›Full record

ArticlePlant physiology2011

Assembly and sorting of the tonoplast potassium channel AtTPK1 and its turnover by internalization into the vacuole.

Marie Maîtrejean, Michael M Wudick, Camilla Voelker, Bhakti Prinsi, Bernd Mueller-Roeber, Katrin Czempinski, Emanuela Pedrazzini, Alessandro Vitale

Open access · hybridAbstract read
In one paragraph

Article in Plant physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 43 citations in OpenAlex.

  1. Condensate-mediated shape transformations of cellular membranes by capillary forces.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
  2. The fate and function of theFrontiers in plant science · 2025
    Article
  3. Protein Biosynthesis and Maturation in the ER.Methods in molecular biology (Clifton, N.J.) · 2024
    Article
  4. Article
  5. New Insights into Plant TPK Ion Channel Evolution.Plants (Basel, Switzerland) · 2021
    Article
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. The glycan-dependent ERAD machinery degrades topologically diverse misfolded proteins.The Plant journal : for cell and molecular biology · 2018
    Article
  15. Article
  16. Phosphatidylinositol 3-phosphate-binding protein AtPH1 controls the localization of the metal transporter NRAMP1 inProceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  17. Article
  18. Article
  19. K₂p channels in plants and animals.Pflugers Archiv : European journal of physiology · 2015
    Review
  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

8 authors at 3 institutions in 2 countries.

Marie MaîtrejeanIstituto di Biologia e Biotecnologia Agraria, Consiglio Nazionale delle Ricerche, 20133 Milan, Italy.
Michael M Wudick
Camilla Voelker
Bhakti Prinsi
Bernd Mueller-Roeber
Katrin Czempinski
Emanuela Pedrazzini
Alessandro Vitale
University of Milan · ITDeleted InstitutionIstituto di Biologia e Biotecnologia Agraria · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The assembly, sorting signals, and turnover of the tonoplast potassium channel AtTPK1 of Arabidopsis (Arabidopsis thaliana) were studied. We used transgenic Arabidopsis expressing a TPK1-green fluorescent protein (GFP) fusion or protoplasts transiently transformed with chimeric constructs based on domain exchange between TPK1 and TPK4, the only TPK family member not located at the tonoplast. The results show that TPK1-GFP is a dimer and that the newly synthesized polypeptides transiently interact with a thus-far unidentified 20-kD polypeptide. A subset of the TPK1-TPK4 chimeras were unable to assemble correctly and these remained located in the endoplasmic reticulum where they interacted with the binding protein chaperone. Therefore, TPK1 must assemble correctly to pass endoplasmic reticulum quality control. Substitution of the cytosolic C terminus of TPK4 with the corresponding domain of TPK1 was sufficient to allow tonoplast delivery, indicating that this domain contains tonoplast sorting information. Pulse-chase labeling indicated that TPK1-GFP has a half-life of at least 24 h. Turnover of the fusion protein involves internalization into the vacuole where the GFP domain is released. This indicates a possible mechanism for the turnover of tonoplast proteins.

Indexed as

EndocytosisArabidopsisArabidopsis ProteinsCytosolEndoplasmic ReticulumGreen Fluorescent ProteinsMolecular WeightPeptidesPlants, Genetically ModifiedPotassium ChannelsPotassium Channels, Tandem Pore DomainProtein BindingProtein MultimerizationProtein Structure, TertiaryProtein TransportRecombinant Fusion ProteinsArabidopsis ProteinsGreen Fluorescent ProteinsKCO1 protein, ArabidopsisPeptidesPotassium ChannelsPotassium Channels, Tandem Pore DomainRecombinant Fusion Proteins

Identifiers

PMID21697507
PMCPMC3149923
OpenAlexW1984672950

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.