Evidence map›Paper›PMID 20876570›Full record

ArticleThe Journal of biological chemistry2010

Functional complementation and genetic deletion studies of KirBac channels: activatory mutations highlight gating-sensitive domains.

Jennifer J Paynter, Isabelle Andres-Enguix, Philip W Fowler, Stephen Tottey, Wayland Cheng, Decha Enkvetchakul, Vassiliy N Bavro, Yoshio Kusakabe, Mark S P Sansom, Nigel J Robinson and 2 more

Abstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. 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
–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

21 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. The Lipid Activation Mechanism of a Transmembrane Potassium Channel.Journal of the American Chemical Society · 2020
    Article
  7. Conduction through a narrow inward-rectifier KThe Journal of general physiology · 2019
    Article
  8. International journal of molecular sciences · 2019
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  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

12 authors.

Jennifer J PaynterDepartment of Physiology, Anatomy and Genetics, University of Oxford, Oxford OX1 3PU, United Kingdom.
Isabelle Andres-Enguix
Philip W Fowler
Stephen Tottey
Wayland Cheng
Decha Enkvetchakul
Vassiliy N Bavro
Yoshio Kusakabe
Mark S P Sansom
Nigel J Robinson
Colin G Nichols
Stephen J Tucker

Funding

Rectification &Block of Ion Channel CurrentsR01HL054171 · NHLBI · WASHINGTON UNIVERSITY · PI NICHOLS, COLIN G · 1995 to 2017
$4.5M
Phospholipid and proton modulation of KirBac1.1 channel acitivityR01DK069424 · NIDDK · WASHINGTON UNIVERSITY · PI ENKVETCHAKUL, DECHA · 2006 to 2010
$1.1M
Biotechnology and Biological Sciences Research Council BB/F013035/1Biotechnology and Biological Sciences Research Council BB/H006052/1British Heart Foundation PG/09/016/26992NHLBI NIH HHS HL54171NHLBI NIH HHS R01 HL054171NIDDK NIH HHS DK069424NIDDK NIH HHS R01 DK069424Wellcome Trust 084655
6 · The paper itself

Abstract

The superfamily of prokaryotic inwardly rectifying (KirBac) potassium channels is homologous to mammalian Kir channels. However, relatively little is known about their regulation or about their physiological role in vivo. In this study, we have used random mutagenesis and genetic complementation in K(+)-auxotrophic Escherichia coli and Saccharomyces cerevisiae to identify activatory mutations in a range of different KirBac channels. We also show that the KirBac6.1 gene (slr5078) is necessary for normal growth of the cyanobacterium Synechocystis PCC6803. Functional analysis and molecular dynamics simulations of selected activatory mutations identified regions within the slide helix, transmembrane helices, and C terminus that function as important regulators of KirBac channel activity, as well as a region close to the selectivity filter of KirBac3.1 that may have an effect on gating. In particular, the mutations identified in TM2 favor a model of KirBac channel gating in which opening of the pore at the helix-bundle crossing plays a far more important role than has recently been proposed.

Indexed as

Genetic Complementation TestMutationEscherichia coliEscherichia coli ProteinsIon Channel GatingPotassium Channels, Inwardly RectifyingProtein Structure, SecondaryProtein Structure, TertiarySaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSynechocystisEscherichia coli ProteinsPotassium Channels, Inwardly RectifyingSaccharomyces cerevisiae Proteins

Identifiers

PMID20876570
PMCPMC3003375

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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.