Evidence map›Paper›PMID 11711561›Full record

ArticleThe Journal of physiology2001

Alternative splicing determines sensitivity of murine calcium-activated potassium channels to glucocorticoids.

L Tian, M S Hammond, H Florance, F A Antoni, M J Shipston

Open access · greenAbstract read
In one paragraph

Article in The Journal of physiology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
0.9field-weighted citation impact, top 27% 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

23 citing papers in PubMed, 56 citations in OpenAlex.

  1. Review
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  11. Intron retention facilitates splice variant diversity in calcium-activated big potassium channel populations.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  12. Review
  13. Article
  14. Article
  15. Colonic potassium handling.Pflugers Archiv : European journal of physiology · 2010
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Review
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 at 1 institution in 1 country.

L TianMembrane Biology Group and MRC "Membrane and Adapter Protein" COOP, Section of Biomedical Sciences, University of Edinburgh Medical School, Hugh Robson Building, Edinburgh EH8 9XD, UK.
M S Hammond
H Florance
F A Antoni
M J Shipston
University of Edinburgh · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

1. Large-conductance Ca(2+)- and voltage-activated potassium (BK) channels are important regulators of cellular excitability. Here, we present a patch-clamp electrophysiological analysis of splice-variant-specific regulation by the synthetic glucocorticoid dexamethasone (DEX) of BK channels consisting of cloned STREX or ZERO alpha-subunit variants expressed in human embryonic kidney (HEK 293) cells. 2. STREX channels in isolated membrane patches were inhibited by protein kinase A (PKA) and this was blocked on pre-treatment of intact cells with DEX (100 nM) for 2 h. 3. The effect of DEX required the synthesis of new mRNA and protein. Furthermore, it required protein phosphatase 2A (PP2A)-like activity intimately associated with the channels, as it was blocked by 10 nM okadaic acid but not by the specific protein phosphatase-1 inhibitor peptide PPI-2. 4. ZERO variant channels that lack the STREX insert were activated by PKA but were not influenced by DEX. ZERO channels containing a mutant STREX domain (S4(STREX)A) were also activated by PKA. Importantly, DEX blocked PKA activation of S4(STREX)A channels in a PP2A-dependent manner. 5. Taken together, the STREX domain is crucial for glucocorticoid regulation of BK channels through a PP2A-type enzyme. Moreover, glucocorticoids appear to induce a generic set of proteins in different types of cells, the actions of which depend on the expression of cell-specific targets.

Indexed as

Alternative SplicingAnimalsCell LineCyclic AMP-Dependent Protein KinasesDexamethasoneGlucocorticoidsHumansLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsMicePhosphoprotein PhosphatasesPotassium Channel BlockersPotassium ChannelsPotassium Channels, Calcium-ActivatedProtein BiosynthesisProtein IsoformsCyclic AMP-Dependent Protein KinasesDexamethasoneGlucocorticoidsLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsLarge-Conductance Calcium-Activated Potassium ChannelsPhosphoprotein PhosphatasesPotassium Channel BlockersPotassium ChannelsPotassium Channels, Calcium-ActivatedProtein IsoformsProtein Phosphatase 1Protein Phosphatase 2Receptors, GlucocorticoidRNA, Messenger

Identifiers

PMID11711561
PMCPMC2278927
OpenAlexW2033707567

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.