Evidence map›Paper›PMID 16549765›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

Defining the BK channel domains required for beta1-subunit modulation.

John P Morrow, Sergey I Zakharov, Guoxia Liu, Lin Yang, Andrea J Sok, Steven O Marx

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
1.9field-weighted citation impact, top 16% 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

52 citing papers in PubMed, 75 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Calcium-Activated KHandbook of experimental pharmacology · 2021
    Article
  7. Comparative gain-of-function effects of theJournal of neurophysiology · 2020
    Article
  8. The Journal of general physiology · 2019
    Review
  9. The Journal of biological chemistry · 2019
    Article
  10. Article
  11. Tyrphostin AG556 increases the activity of large conductance CaJournal of cellular and molecular medicine · 2017
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. β1-subunit-induced structural rearrangements of the Ca2+- and voltage-activated K+ (BK) channel.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  17. Review
  18. Article
  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

6 authors at 1 institution in 1 country.

John P MorrowDivision of Cardiology, Department of Medicine, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
Sergey I Zakharov
Guoxia Liu
Lin Yang
Andrea J Sok
Steven O Marx
Columbia University · US

Funding

POSTDOCTORAL TRAINING IN CARDIOVASCULAR DISEASET32HL007854 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI Marwah Abdalla, Michael Argenziano · 1996 to 2026
$14.7M
Ion channel regulation by macromolecular complexesR01HL068093 · NHLBI · COLUMBIA UNIVERSITY HEALTH SCIENCES · PI MARX, STEVEN O · 2001 to 2010
$2.4M
NHLBI NIH HHS HL068093NHLBI NIH HHS R01 HL068093NHLBI NIH HHS T32 HL007854
6 · The paper itself

Abstract

In a wide variety of cell types, including neurons and smooth muscle cells, activation of the large-conductance voltage- and Ca(2+)-activated K(+) (BK) channels causes transient membrane hyperpolarization, thereby regulating cellular excitability. Similar to other voltage-gated ion channels, BK channels, a tetramer of alpha-subunits, associate with auxiliary beta-subunits in a tissue-specific manner, modifying the channel's gating properties. The BK beta1-subunit, which is expressed in smooth muscle, increases the apparent Ca(2+) sensitivity (marked by a hyperpolarizing shift in the conductance-voltage relationship at a given Ca(2+) concentration), slows macroscopic activation and deactivation, and is required for channel activation by 17beta-estradiol. The beta1-subunit is essential for normal regulation of vascular smooth muscle contractility and blood pressure. Little is known, however, about the molecular mechanisms of beta1-subunit modulation of alpha-subunits. Here we show that the beta1-subunit's modulation of the Ca(2+) and 17beta-estradiol sensitivities can be dissociated from its effects on gating kinetics by truncation of the alpha-subunit's extracellular N-terminal residues. The BK alpha-subunit N terminus interacts uniquely with the beta1-subunit: beta2 regulation of the alpha-subunit is unaltered by truncation of the N terminus. Although the functional interaction of alpha and beta1 requires the N-terminal tail of alpha, the physical association requires the S1, S2, and S3 transmembrane helices of alpha.

Indexed as

Amino Acid SequenceAnimalsCell LineElectrophysiologyEstradiolHumansIon Channel GatingKineticsMiceMolecular Sequence DataMutationPatch-Clamp TechniquesPotassium Channels, Calcium-ActivatedProtein BindingProtein Structure, TertiaryProtein SubunitsEstradiolPotassium Channels, Calcium-ActivatedProtein Subunits

Identifiers

PMID16549765
PMCPMC1458800
OpenAlexW2006423698

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.