Evidence map›Paper›PMID 22049343›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2011

Alternatively spliced domains interact to regulate BK potassium channel gating.

Brandon E Johnson, Dominique A Glauser, Elise S Dan-Glauser, D Brent Halling, Richard W Aldrich, Miriam B Goodman

Abstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.

0numbers the graph read from it
0cells of the map it votes in
30citing 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

30 citing papers in PubMed.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. A Novel Peptide Restricts Ethanol Modulation of the BK Channel In Vitro and In Vivo.The Journal of pharmacology and experimental therapeutics · 2018
    Article
  8. Article
  9. Article
  10. Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017
    Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Conserved single residue in the BK potassium channel required for activation by alcohol and intoxication in C. elegans.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  18. Article
  19. Review
  20. Review
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

6 authors.

Brandon E JohnsonDepartment of Molecular and Cellular Physiology, Stanford University, Stanford, CA 94305, USA.
Dominique A Glauser
Elise S Dan-Glauser
D Brent Halling
Richard W Aldrich
Miriam B Goodman

Funding

Molecular Basis of Sensory Transduction in C. elegansR01NS047715 · NINDS · STANFORD UNIVERSITY · PI GOODMAN, MIRIAM B · 2004 to 2017
$4.9M
Temperature Sensation and Its Behavioral ConsequencesR21NS061147 · NINDS · STANFORD UNIVERSITY · PI GOODMAN, MIRIAM B · 2007 to 2008
$380k
NINDS NIH HHS NS047715NINDS NIH HHS NS061147NINDS NIH HHS R01 NS047715NINDS NIH HHS R21 NS061147
6 · The paper itself

Abstract

Most human genes contain multiple alternative splice sites believed to extend the complexity and diversity of the proteome. However, little is known about how interactions among alternative exons regulate protein function. We used the Caenorhabditis elegans slo-1 large-conductance calcium and voltage-activated potassium (BK) channel gene, which contains three alternative splice sites (A, B, and C) and encodes at least 12 splice variants, to investigate the functional consequences of alternative splicing. These splice sites enable the insertion of exons encoding part of the regulator of K(+) conductance (RCK)1 Ca(2+) coordination domain (exons A1 and A2) and portions of the RCK1-RCK2 linker (exons B0, B1, B2, C0, and C1). Exons A1 and A2 are used in a mutually exclusive manner and are 67% identical. The other exons can extend the RCK1-RCK2 linker by up to 41 residues. Electrophysiological recordings of all isoforms show that the A1 and A2 exons regulate activation kinetics and Ca(2+) sensitivity, but only if alternate exons are inserted at site B or C. Thus, RCK1 interacts with the RCK1-RCK2 linker, and the effect of exon variation on gating depends on the combination of alternate exons present in each isoform.

Indexed as

Alternative SplicingAnimalsBiophysicsCaenorhabditis elegansElectrophysiologyExonsGenetic VariationKineticsLarge-Conductance Calcium-Activated Potassium ChannelsModels, GeneticOocytesProtein Structure, TertiaryXenopusLarge-Conductance Calcium-Activated Potassium Channels

Identifiers

PMID22049343
PMCPMC3251094

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.