Evidence map›Paper›PMID 10423425›Full record

ArticleBiophysical journal1999

Evolutionary relationship between K(+) channels and symporters.

S R Durell, Y Hao, T Nakamura, E P Bakker, H R Guy

Abstract readComparative Study
In one paragraph

Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
–field-weighted citation impact
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

65 citing papers in PubMed.

  1. Article
  2. Article
  3. A High-KInternational journal of molecular sciences · 2023
    Article
  4. Dimerisation of the Yeast KInternational journal of molecular sciences · 2022
    Article
  5. Review
  6. Review
  7. A Novel High-Affinity Potassium TransporterPlants (Basel, Switzerland) · 2022
    Article
  8. International journal of molecular sciences · 2022
    Review
  9. Article
  10. Review
  11. Review
  12. Cation Transporters ofBiomolecules · 2021
    Review
  13. Article
  14. Article
  15. Overexpression ofGenes · 2018
    Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Article

5 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

5 authors.

S R DurellLaboratory of Experimental and Computational Biology, Division of Basic Sciences, National Cancer Institute, National Institutes of Health, Bethesda, Maryland 20892-5677, USA.
Y Hao
T Nakamura
E P Bakker
H R Guy

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The hypothesis is presented that at least four families of putative K(+) symporter proteins, Trk and KtrAB from prokaryotes, Trk1,2 from fungi, and HKT1 from wheat, evolved from bacterial K(+) channel proteins. Details of this hypothesis are organized around the recently determined crystal structure of a bacterial K(+) channel: i. e., KcsA from Streptomyces lividans. Each of the four identical subunits of this channel has two fully transmembrane helices (designated M1 and M2), plus an intervening hairpin segment that determines the ion selectivity (designated P). The symporter sequences appear to contain four sequential M1-P-M2 motifs (MPM), which are likely to have arisen from gene duplication and fusion of the single MPM motif of a bacterial K(+) channel subunit. The homology of MPM motifs is supported by a statistical comparison of the numerical profiles derived from multiple sequence alignments formed for each protein family. Furthermore, these quantitative results indicate that the KtrAB family of symporters has remained closest to the single-MPM ancestor protein. Strong sequence evidence is also found for homology between the cytoplasmic C-terminus of numerous bacterial K(+) channels and the cytoplasm-resident TrkA and KtrA subunits of the Trk and KtrAB symporters, which in turn are homologous to known dinucleotide-binding domains of other proteins. The case for homology between bacterial K(+) channels and the four families of K(+) symporters is further supported by the accompanying manuscript, in which the patterns of residue conservation are demonstrated to be similar to each other and consistent with the known 3D structure of the KcsA K(+) channel.

Indexed as

Cation Transport ProteinsEvolution, MolecularSaccharomyces cerevisiae ProteinsSymportersAmino Acid SequenceBacterial ProteinsBinding SitesBiophysical PhenomenaBiophysicsCarrier ProteinsConserved SequenceFungal ProteinsMembrane ProteinsMolecular Sequence DataOligonucleotidesPlant ProteinsBacterial ProteinsCarrier ProteinsCation Transport ProteinsFungal ProteinsHKT1 protein, plantKtrB protein, BacteriaMembrane ProteinsOligonucleotidesPlant ProteinsPotassium Channelsprokaryotic potassium channelSaccharomyces cerevisiae ProteinsSymportersTRK1 protein, S cerevisiae

Identifiers

PMID10423425
PMCPMC1300371

What OpenQuestion holds

Textmetadata
Read underepoch 390

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.