Evidence map›Paper›PMID 11723163›Full record

ArticleThe Journal of general physiology2001

Gating and conductance properties of BK channels are modulated by the S9-S10 tail domain of the alpha subunit. A study of mSlo1 and mSlo3 wild-type and chimeric channels.

B L Moss, K L Magleby

Abstract read
In one paragraph

Article in The Journal of general physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
–field-weighted citation impact
1 · What the graph read from it

What it found

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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

20 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Modes of operation of the BKCa channel beta2 subunit.The Journal of general physiology · 2007
    Article
  8. Article
  9. Article
  10. Article
  11. Opposite regulation of Slick and Slack K+ channels by neuromodulators.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006
    Article
  12. Article
  13. Electrophysiological characterization of C-terminal Kv4 channel fusion proteins.Pflugers Archiv : European journal of physiology · 2005
    Article
  14. Ligand-dependent activation of Slo family channels is defined by interchangeable cytosolic domains.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004
    Article
  15. Article
  16. A ring of eight conserved negatively charged amino acids doubles the conductance of BK channels and prevents inward rectification.Proceedings of the National Academy of Sciences of the United States of America · 2003
    Article
  17. Gating mechanism of BK (Slo1) channels: so near, yet so far.The Journal of general physiology · 2003
    Review
  18. Article
  19. Stepwise contribution of each subunit to the cooperative activation of BK channels by Ca2+.Proceedings of the National Academy of Sciences of the United States of America · 2002
    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

2 authors.

B L MossDepartment of Physiology and Biophysics, University of Miami School of Medicine, Miami, FL 33101-6430, USA.
K L Magleby

Funding

MECHANISMS OF IONIC CHANNEL ACTIVITYR01AR032805 · NIAMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MAGLEBY, KARL L · 1986 to 2012
$4.3M
MECHANISMS OF IONIC CHANNEL ACTIVITYR37AR032805 · NIAMS · UNIVERSITY OF MIAMI SCHOOL OF MEDICINE · PI MAGLEBY, KARL L · 1988 to 1997
–
NIAMS NIH HHS AR32805NIAMS NIH HHS R01 AR032805
6 · The paper itself

Abstract

The COOH-terminal S9-S10 tail domain of large conductance Ca(2+)-activated K(+) (BK) channels is a major determinant of Ca(2+) sensitivity (Schreiber, M., A. Wei, A. Yuan, J. Gaut, M. Saito, and L. Salkoff. 1999. Nat. Neurosci. 2:416-421). To investigate whether the tail domain also modulates Ca(2+)-independent properties of BK channels, we explored the functional differences between the BK channel mSlo1 and another member of the Slo family, mSlo3 (Schreiber, M., A. Yuan, and L. Salkoff. 1998. J. Biol. Chem. 273:3509-3516). Compared with mSlo1 channels, mSlo3 channels showed little Ca(2+) sensitivity, and the mean open time, burst duration, gaps between bursts, and single-channel conductance of mSlo3 channels were only 32, 22, 41, and 37% of that for mSlo1 channels, respectively. To examine which channel properties arise from the tail domain, we coexpressed the core of mSlo1 with either the tail domain of mSlo1 or the tail domain of mSlo3 channels, and studied the single-channel currents. Replacing the mSlo1 tail with the mSlo3 tail resulted in the following: increased open probability in the absence of Ca(2+); reduced the Ca(2+) sensitivity greatly by allowing only partial activation by Ca(2+) and by reducing the Hill coefficient for Ca(2+) activation; decreased the voltage dependence approximately 28%; decreased the mean open time two- to threefold; decreased the mean burst duration three- to ninefold; decreased the single-channel conductance approximately 14%; decreased the K(d) for block by TEA(i) approximately 30%; did not change the minimal numbers of three to four open and five to seven closed states entered during gating; and did not change the major features of the dependency between adjacent interval durations. These observations support a modular construction of the BK channel in which the tail domain modulates the gating kinetics and conductance properties of the voltage-dependent core domain, in addition to determining most of the high affinity Ca(2+) sensitivity.

Indexed as

Potassium Channels, Calcium-ActivatedAnimalsCalciumCell Culture TechniquesElectrophysiologyFemaleIon Channel GatingKineticsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsModels, TheoreticalOocytesPotassium ChannelsXenopus laevisCalciumLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPotassium ChannelsPotassium Channels, Calcium-Activated

Identifiers

PMID11723163
PMCPMC2229511

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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.