Evidence map›Paper›PMID 15075266›Full record

ArticleEukaryotic cell2004

Novel p-type ATPases mediate high-affinity potassium or sodium uptake in fungi.

Begoña Benito, Blanca Garciadeblás, Peter Schreier, Alonso Rodríguez-Navarro

Open access · diamondAbstract read
In one paragraph

Article in Eukaryotic cell, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.

0numbers the graph read from it
0cells of the map it votes in
33citing papers in PubMed
4.8field-weighted citation impact, top 5% 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

33 citing papers in PubMed, 74 citations in OpenAlex.

  1. Biology · 2026
    Article
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  3. Mutational analysis of an antimalarial drug target,Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  4. Article
  5. Article
  6. International journal of molecular sciences · 2022
    Review
  7. Article
  8. The Potassium Transporter Hak1 inJournal of fungi (Basel, Switzerland) · 2021
    Article
  9. P-type NaVirulence · 2020
    Article
  10. Article
  11. Article
  12. The Role of Soil Fungi in KInternational journal of molecular sciences · 2019
    Review
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  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

4 authors at 2 institutions in 2 countries.

Begoña BenitoDepartamento de Biotecnología, Universidad Politécnica de Madrid, 28040 Madrid, Spain. Bayer CropScience R-TRF, 40789 Monheim, Germany.
Blanca Garciadeblás
Peter Schreier
Alonso Rodríguez-Navarro
Universidad Politécnica de Madrid · ESBayer (Germany) · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Fungi have an absolute requirement for K+, but K+ may be partially replaced by Na+. Na+ uptake in Ustilago maydis and Pichia sorbitophila was found to exhibit a fast rate, low Km, and apparent independence of the membrane potential. Searches of sequences with similarity to P-type ATPases in databases allowed us to identify three genes in these species, Umacu1, Umacu2, and PsACU1, that could encode P-type ATPases of a novel type. Deletion of the acu1 and acu2 genes proved that they encoded the transporters that mediated the high-affinity Na+ uptake of U. maydis. Heterologous expressions of the Umacu2 gene in K+ transport mutants of Saccharomyces cerevisiae and transport studies in the single and double Deltaacu1 and Deltaacu2 mutants of U. maydis revealed that the acu1 and acu2 genes encode transporters that mediated high-affinity K+ uptake in addition to Na+ uptake. Other fungi also have genes or pseudogenes whose translated sequences show high similarity to the ACU proteins of U. maydis and P. sorbitophila. In the phylogenetic tree of P-type ATPases all the identified ACU ATPases define a new cluster, which shows the lowest divergence with type IIC, animal Na+,K(+)-ATPases. The fungal high-affinity Na+ uptake mediated by ACU ATPases is functionally identical to the uptake that is mediated by some plant HKT transporters.

Indexed as

Adenosine TriphosphatasesAmino Acid SequenceFungal ProteinsFungiIon TransportMolecular Sequence DataPhylogenyPichiaPotassiumSequence AlignmentSequence DeletionSodiumUstilagoAdenosine TriphosphatasesFungal ProteinsPotassiumSodium

Identifiers

PMID15075266
PMCPMC387655
OpenAlexW2146618203

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.