Evidence map›Paper›PMID 20519529›Full record

ArticleThe Journal of neuroscience : the official journal of the Society for Neuroscience2010

The RCK2 domain uses a coordination site present in Kir channels to confer sodium sensitivity to Slo2.2 channels.

Zhe Zhang, Avia Rosenhouse-Dantsker, Qiong-Yao Tang, Sergei Noskov, Diomedes E Logothetis

Abstract read
In one paragraph

Article in The Journal of neuroscience : the official journal of the Society for Neuroscience, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing 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

48 citing papers in PubMed.

  1. Article
  2. Review
  3. TrkA ofMicrobiology (Reading, England) · 2025
    Article
  4. Andrology · 2025
    Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. The Slack Channel Regulates Anxiety-Like Behaviors via Basolateral Amygdala Glutamatergic Projections to Ventral Hippocampus.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022
    Article
  15. Review
  16. Double-edged Role of KCurrent neuropharmacology · 2022
    Review
  17. Article
  18. Review
  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

5 authors.

Zhe ZhangDepartment of Physiology and Biophysics, Virginia Commonwealth University, School of Medicine, Richmond, Virginia 23298-0551, USA.
Avia Rosenhouse-Dantsker
Qiong-Yao Tang
Sergei Noskov
Diomedes E Logothetis

Funding

Structural Determinants of PIP2 RegulationR01HL059949 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI Leigh Daniel Plant · 1998 to 2026
$11.6M
Modulation of Kir Channel Function by PhosphorylationR01HL090882 · NHLBI · VIRGINIA COMMONWEALTH UNIVERSITY · PI LOGOTHETIS, DIOMEDES E. · 2009 to 2012
$1.5M
CIHR MOP-186232NHLBI NIH HHS HL059949-11NHLBI NIH HHS HL090882-01NHLBI NIH HHS R01 HL059949NHLBI NIH HHS R01 HL090882
6 · The paper itself

Abstract

Slo2 Na(+)-activated potassium channels are widely expressed in neurons and other cells, such as kidney, heart, and skeletal muscle. Although their important physiological roles continue to be appreciated, molecular determinants responsible for sensing intracellular Na(+) remain unknown. Here we report identification of an Na(+) regulatory site, similar to an Na(+) coordination motif described in Kir channels, localized in the RCK2 domain of Slo2.2 channels. Molecular simulations of the homology-modeled Slo2.2 RCK2 domain provided structural insights into the organization of this Na(+) coordination site. Furthermore, free energy calculations reproduced the experimentally derived monovalent cation selectivity. Our results suggest that Slo2.2 and Kir channels share a similar mechanism to coordinate Na(+). The localization of an Na(+) sensor within the RCK2 domain of Slo2.2 further supports the role of RCK (regulators of conductance of K(+)) domains of Slo channels in coupling ion sensing to channel gating.

Indexed as

Amino AcidsAmino Acid SequenceAnimalsBiophysical PhenomenaChloridesDose-Response Relationship, DrugElectric StimulationG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIntermediate-Conductance Calcium-Activated Potassium ChannelsIon Channel GatingKv1.6 Potassium ChannelMembrane PotentialsMicroinjectionsModels, MolecularMolecular Sequence DataMutationAmino AcidsChloridesG Protein-Coupled Inwardly-Rectifying Potassium ChannelsIntermediate-Conductance Calcium-Activated Potassium ChannelsKv1.6 Potassium ChannelSodium

Identifiers

PMID20519529
PMCPMC3277328

What OpenQuestion holds

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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.