Evidence map›Paper›PMID 20865173›Full record

ArticlePLoS genetics2010

An alpha-catulin homologue controls neuromuscular function through localization of the dystrophin complex and BK channels in Caenorhabditis elegans.

Linu S Abraham, Hyun J Oh, Feyza Sancar, Janet E Richmond, Hongkyun Kim

Open access · goldAbstract read
In one paragraph

Article in PLoS genetics, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.8field-weighted citation impact, top 32% 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

23 citing papers in PubMed, 31 citations in OpenAlex.

  1. Potential therapeutic targeting of BKMolecular oncology · 2026
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  4. Regulation of Neurotransmitter Release by KAdvances in neurobiology · 2023
    Article
  5. Review
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  7. Article
  8. Article
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  10. Review
  11. HRPU-2, a Homolog of Mammalian hnRNP U, Regulates Synaptic Transmission by Controlling the Expression of SLO-2 Potassium Channel inThe Journal of neuroscience : the official journal of the Society for Neuroscience · 2018
    Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
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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 1 country.

Linu S AbrahamDepartment of Cell Biology and Anatomy, The Chicago Medical School, Rosalind Franklin University of Medicine and Science, North Chicago, Illinois, United States of America.
Hyun J Oh
Feyza Sancar
Janet E Richmond
Hongkyun Kim
Franklin University · USUniversity of Illinois Chicago · USRosalind Franklin University of Medicine and Science · US

Funding

The role of tomosyn in synaptic transmission.R01MH073156 · NIMH · UNIVERSITY OF ILLINOIS AT CHICAGO · PI RICHMOND, JANET E · 2006 to 2010
$2.0M
Identification of Novel Components of the Dystrophin Complex Using C. ElegansR01NS058814 · NINDS · ROSALIND FRANKLIN UNIV OF MEDICINE & SCI · PI KIM, HONGKYUN · 2007 to 2010
$1.1M
NIMH NIH HHS R01 MH073156NINDS NIH HHS R01 NS058814
6 · The paper itself

Abstract

The large conductance, voltage- and calcium-dependent potassium (BK) channel serves as a major negative feedback regulator of calcium-mediated physiological processes and has been implicated in muscle dysfunction and neurological disorders. In addition to membrane depolarization, activation of the BK channel requires a rise in cytosolic calcium. Localization of the BK channel near calcium channels is therefore critical for its function. In a genetic screen designed to isolate novel regulators of the Caenorhabditis elegans BK channel, SLO-1, we identified ctn-1, which encodes an α-catulin homologue with homology to the cytoskeletal proteins α-catenin and vinculin. ctn-1 Mutants resemble slo-1 loss-of-function mutants, as well as mutants with a compromised dystrophin complex. We determined that CTN-1 uses two distinct mechanisms to localize SLO-1 in muscles and neurons. In muscles, CTN-1 utilizes the dystrophin complex to localize SLO-1 channels near L-type calcium channels. In neurons, CTN-1 is involved in localizing SLO-1 to a specific domain independent of the dystrophin complex. Our results demonstrate that CTN-1 ensures the localization of SLO-1 within calcium nanodomains, thereby playing a crucial role in muscles and neurons.

Indexed as

alpha CateninAnimalsCaenorhabditis elegansCaenorhabditis elegans ProteinsDystrophinLarge-Conductance Calcium-Activated Potassium ChannelsMusclesNeuronsProtein Transportalpha CateninCaenorhabditis elegans ProteinsDystrophinLarge-Conductance Calcium-Activated Potassium Channelsslo-1 protein, C elegans

Identifiers

PMID20865173
PMCPMC2928805
OpenAlexW1981207857

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.