Evidence map›Paper›PMID 18345016›Full record

ArticleNature structural & molecular biology2008

Reciprocal regulation of the Ca2+ and H+ sensitivity in the SLO1 BK channel conferred by the RCK1 domain.

Shangwei Hou, Rong Xu, Stefan H Heinemann, Toshinori Hoshi

Abstract read
In one paragraph

Article in Nature structural & molecular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 42 papers.

0numbers the graph read from it
0cells of the map it votes in
42citing 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

42 citing papers in PubMed.

  1. Article
  2. Redox Regulation of KAntioxidants & redox signaling · 2024
    Review
  3. Review
  4. Article
  5. SLO3: A Conserved Regulator of Sperm Membrane Potential.International journal of molecular sciences · 2023
    Review
  6. Article
  7. Article
  8. BKAntioxidants (Basel, Switzerland) · 2020
    Review
  9. Article
  10. CO-independent modification of KEuropean journal of pharmacology · 2017
    Article
  11. Review
  12. Understanding the conformational motions of RCK gating rings.The Journal of general physiology · 2017
    Review
  13. Atomic determinants of BK channel activation by polyunsaturated fatty acids.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  14. A heme-binding domain controls regulation of ATP-dependent potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  15. Article
  16. Article
  17. Review
  18. Article
  19. Carbon monoxide--physiology, detection and controlled release.Chemical communications (Cambridge, England) · 2014
    Review
  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

4 authors.

Shangwei HouDepartment of Physiology, University of Pennsylvania, 3700 Hamilton Walk, Philadelphia, Pennsylvania 19104, USA.
Rong Xu
Stefan H Heinemann
Toshinori Hoshi

Funding

REGULATION OF ION CHANNELS BY METHIONINE OXIDATIONR01GM057654 · NIGMS · UNIVERSITY OF PENNSYLVANIA · PI HOSHI, TOSHINORI, OLCESE, RICCARDO · 1998 to 2014
$5.0M
NIGMS NIH HHS R01 GM057654
6 · The paper itself

Abstract

Increasing evidence suggests that intracellular H+ directly stimulates large-conductance Ca2+- and voltage-activated K+ (SLO1 BK) channels, thus providing a crucial link between membrane excitability and cell metabolism. Here we report that two histidine residues, His365 and His394, located in the intracellular regulator of conductance for K+ (RCK) 1 domain, serve as the H+ sensors of the SLO1 BK channel. Activation of the channel by H+ requires electrostatic interactions between the histidine residues and a nearby negatively charged residue involved in the channel's high-affinity Ca2+ sensitivity. Reciprocally, His365 and His394 also participate in the Ca2+-dependent activation of the channel, functioning as Ca2+ mimetics once they are protonated. Therefore, a common motif in the RCK1 domain mediates the stimulatory effects of both H+ and Ca2+, and provides a basis for the bidirectional coupling of cell metabolism and membrane electrical excitability.

Indexed as

Amino Acid SequenceAnimalsCalciumDrosophila melanogasterHistidineHumansHydrogenHydrogen-Ion ConcentrationLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMolecular Sequence DataMutationOsmolar ConcentrationRecombinant ProteinsSequence Homology, Amino AcidStatic ElectricityCalciumHistidineHydrogenKCNMA1 protein, humanLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsRecombinant Proteins

Identifiers

PMID18345016
PMCPMC2905141

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

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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.