Evidence map›Paper›PMID 15216418›Full record

ArticleThe Journal of membrane biology2004

Chloride channel function in the yeast TRK-potassium transporters.

T Kuroda, H Bihler, E Bashi, C L Slayman, A Rivetta

Abstract read
PubMed Publisher
In one paragraph

Article in The Journal of membrane biology, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
1.4field-weighted citation impact, top 21% 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

18 citing papers in PubMed, 45 citations in OpenAlex.

  1. Review
  2. Dimerisation of the Yeast KInternational journal of molecular sciences · 2022
    Article
  3. International journal of molecular sciences · 2022
    Review
  4. Cation Transporters ofBiomolecules · 2021
    Review
  5. International journal of molecular sciences · 2019
    Review
  6. Evolutionary engineering inBiotechnology for biofuels · 2019
    Article
  7. Article
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Review
  14. Alkali metal cation transport and homeostasis in yeasts.Microbiology and molecular biology reviews : MMBR · 2010
    Review
  15. Article
  16. Article
  17. Article
  18. 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

5 authors at 3 institutions in 3 countries.

T KurodaDepartment of Cellular and Molecular Physiology, Yale School of Medicine, 333 Cedar Street, New Haven, CT 06520, USA.
H Bihler
E Bashi
C L Slayman
A Rivetta
Yale University · USKarlsruhe Institute of Technology · DEOkayama University · JP

Funding

STRUCTURE AND FUNCTION OF K+ CARRIER-CHANNELS IN YEASTR01GM060696 · NIGMS · YALE UNIVERSITY · PI SLAYMAN, CLIFFORD L · 2000 to 2003
$936k
NIGMS NIH HHS GM-60696
6 · The paper itself

Abstract

The TRK proteins-Trk1p and Trk2p- are the main agents responsible for "active" accumulation of potassium by the yeast Saccharomyces cerevisiae. In previous studies, inward currents measured through those proteins by whole-cell patch-clamping proved very unresponsive to changes of extracellular potassium concentration, although they did increase with extracellular proton concentration-qualitatively as expected for H(+) coupling to K(+) uptake. These puzzling observations have now been explored in greater detail, with the following major findings: a) the large inward TRK currents are not carried by influx of either K(+) or H(+), but rather by an efflux of chloride ions; b) with normal expression levels for Trk1p and Trk2p in potassium-replete cells, the inward TRK currents are contributed approximately half by Trk1p and half by Trk2p; but c) strain background strongly influences the absolute magnitude of these currents, which are nearly twice as large in W303-derived spheroplasts as in S288c-derived cells (same cell-size and identical recording conditions); d) incorporation of mutations that increase cell size (deletion of the Golgi calcium pump, Pmr1p) or that upregulate the TRK2 promoter, can further substantially increase the TRK currents; e) removal of intracellular chloride (e.g., replacement by sulfate or gluconate) reveals small inward currents that are K(+)-dependent and can be enhanced by K(+) starvation; and f) finally, the latter currents display two saturating kinetic components, with preliminary estimates of K(0.5) at 46 micro M [K(+)](out) and 6.8 m M [K(+)](out), and saturating fluxes of approximately 5 m M/min and approximately 10 m M/min (referred to intracellular water). These numbers are compatible with the normal K(+)-transport properties of Trk1p and Trk2p, respectively.

Indexed as

Biological Transport, ActiveCation Transport ProteinsChloride ChannelsChlorineIon Channel GatingMembrane PotentialsMutagenesis, Site-DirectedPotassiumRecombinant ProteinsSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSpecies SpecificityStructure-Activity RelationshipCation Transport ProteinsChloride ChannelsChlorinePotassiumRecombinant ProteinsSaccharomyces cerevisiae ProteinsTRK1 protein, S cerevisiaeTRK2 protein, S cerevisiae

Identifiers

PMID15216418
OpenAlexW1993609466

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.