Evidence map›Paper›PMID 24081981›Full record

ArticleThe Journal of general physiology2013

Calmodulin-dependent activation and inactivation of anoctamin calcium-gated chloride channels.

Kerstin Vocke, Kristin Dauner, Anne Hahn, Anne Ulbrich, Jana Broecker, Sandro Keller, Stephan Frings, Frank Möhrlen

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.

0numbers the graph read from it
0cells of the map it votes in
45citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

45 citing papers in PubMed, 70 citations in OpenAlex.

  1. Review
  2. TMEM16 proteins: CaInternational journal of molecular medicine · 2024
    Review
  3. Review
  4. Article
  5. Polymodal Control of TMEM16x Channels and Scramblases.International journal of molecular sciences · 2022
    Review
  6. Review
  7. Article
  8. CaMolecules and cells · 2021
    Article
  9. Review
  10. Allosteric modulation of alternatively spliced CaProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Simultaneous Loss of NCKX4 and CNG Channel Desensitization Impairs Olfactory Sensitivity.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2017
    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

8 authors at 2 institutions in 1 country.

Kerstin VockeDepartment of Molecular Physiology, Centre for Organismal Studies, Heidelberg University, 69120 Heidelberg, Germany.
Kristin Dauner
Anne Hahn
Anne Ulbrich
Jana Broecker
Sandro Keller
Stephan Frings
Frank Möhrlen
Heidelberg University · DEUniversity of Kaiserslautern · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Calcium-dependent chloride channels serve critical functions in diverse biological systems. Driven by cellular calcium signals, the channels codetermine excitatory processes and promote solute transport. The anoctamin (ANO) family of membrane proteins encodes three calcium-activated chloride channels, named ANO 1 (also TMEM16A), ANO 2 (also TMEM16B), and ANO 6 (also TMEM16F). Here we examined how ANO 1 and ANO 2 interact with Ca(2+)/calmodulin using nonstationary current analysis during channel activation. We identified a putative calmodulin-binding domain in the N-terminal region of the channel proteins that is involved in channel activation. Binding studies with peptides indicated that this domain, a regulatory calmodulin-binding motif (RCBM), provides two distinct modes of interaction with Ca(2+)/calmodulin, one at submicromolar Ca(2+) concentrations and one in the micromolar Ca(2+) range. Functional, structural, and pharmacological data support the concept that calmodulin serves as a calcium sensor that is stably associated with the RCBM domain and regulates the activation of ANO 1 and ANO 2 channels. Moreover, the predominant splice variant of ANO 2 in the brain exhibits Ca(2+)/calmodulin-dependent inactivation, a loss of channel activity within 30 s. This property may curtail ANO 2 activity during persistent Ca(2+) signals in neurons. Mutagenesis data indicated that the RCBM domain is also involved in ANO 2 inactivation, and that inactivation is suppressed in the retinal ANO 2 splice variant. These results advance the understanding of Ca(2+) regulation in anoctamin Cl(-) channels and its significance for the physiological function that anoctamin channels subserve in neurons and other cell types.

Indexed as

Action PotentialsAmino Acid SequenceAnimalsAnoctamin-1AnoctaminsBinding SitesBrainCalciumCalmodulinChloride ChannelsHEK293 CellsHumansIon Channel GatingMiceMolecular Sequence DataMutationANO1 protein, ratAno2 protein, ratAnoctamin-1AnoctaminsCalciumCalmodulinChloride ChannelsProtein Isoforms

Identifiers

PMID24081981
PMCPMC3787769
OpenAlexW2133393997

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.