Evidence map›Paper›PMID 19052171›Full record

ArticleMolecular pharmacology2009

Canonical transient receptor potential channel (TRPC)3 and TRPC6 associate with large-conductance Ca2+-activated K+ (BKCa) channels: role in BKCa trafficking to the surface of cultured podocytes.

Eun Young Kim, Claudia P Alvarez-Baron, Stuart E Dryer

Open access · greenAbstract readComparative Study
In one paragraph

Article in Molecular pharmacology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
55citing papers in PubMed, 1 pooled it
3.3field-weighted citation impact, top 8% 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

55 citing papers in PubMed, 1 synthesis or guideline pooled it, 105 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
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  5. Review
  6. Article
  7. Article
  8. Article
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  11. Article
  12. Article
  13. Mechanism of Regulation of Big-Conductance CaFrontiers in physiology · 2019
    Article
  14. Hypoxia selectively upregulates cation channels and increases cytosolic [CaAmerican journal of physiology. Cell physiology · 2018
    Article
  15. Review
  16. Stressed podocytes-mechanical forces, sensors, signaling and response.Pflugers Archiv : European journal of physiology · 2017
    Review
  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

3 authors at 1 institution in 1 country.

Eun Young KimDepartment of Biology and Biochemistry, University of Houston, Houston, TX 77204-5001, USA.
Claudia P Alvarez-Baron
Stuart E Dryer
University of Houston · US

Funding

UC Davis/NIH NeuroMab FacilityU24NS050606 · NINDS · UNIVERSITY OF CALIFORNIA DAVIS · PI TRIMMER, JAMES S · 2005 to 2014
$15.6M
DEVELOPMENT OF IONIC CHANNELSR01NS032748 · NINDS · UNIVERSITY OF HOUSTON · PI DRYER, STUART E. · 1995 to 2005
$1.6M
NINDS NIH HHS R01 NS032748NINDS NIH HHS U24-NS050606
6 · The paper itself

Abstract

Large-conductance (BK(Ca) type) Ca(2+)-activated K(+) channels encoded by the Slo1 gene and various canonical transient receptor potential channels (TRPCs) are coexpressed in many cell types, including podocytes (visceral epithelial cells) of the renal glomerulus. In this study, we show by coimmunoprecipitation and GST pull-down assays that BK(Ca) channels can associate with endogenous TRPC3 and TRPC6 channels in differentiated cells of a podocyte cell line. Both types of TRPC channels colocalize with Slo1 in podocytes and in human embryonic kidney (HEK) 293T cells transiently coexpressing the TRPC channels with Slo1. In HEK293T cells, coexpression of TRPC6 increased surface expression of a Slo1 subunit splice variant (Slo1(VEDEC)) that is typically retained in intracellular compartments, as assessed by cell-surface biotinylation assays and confocal microscopy. Corresponding currents through BK(Ca) channels were also increased with TRPC6 coexpression, as assessed by whole-cell and excised inside-out patch recordings. By contrast, coexpression of TRPC3 had no effect on the surface expression of BK(Ca) channels in HEK293T cells or on the amplitudes of currents in whole cells or excised patches. In podocytes, small interfering RNA knockdown of endogenous TRPC6 reduced steady-state surface expression of endogenous Slo1 channels, but knockdown of TRPC3 had no effect. TRPC6, but not TRPC3 knockdown also reduced voltage-evoked outward current through podocyte BK(Ca) channels. These data indicate that TRPC6 and TRPC3 channels can bind to Slo1, and this colocalization may allow them to serve as a source of Ca(2+) for the activation of BK(Ca) channels. TRPC6 channels also play a role in the regulation of surface expression of a subset of podocyte BK(Ca) channels.

Indexed as

AnimalsCell LineCell MembraneCell Membrane PermeabilityCells, CulturedCytosolHumansIon Channel GatingLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsMicePodocytesProtein BindingProtein Structure, TertiaryProtein SubunitsProtein TransportTRPC6 Cation ChannelKCNMA1 protein, humanLarge-Conductance Calcium-Activated Potassium Channel alpha SubunitsProtein SubunitsTRPC3 cation channelTRPC6 Cation ChannelTRPC6 protein, humanTRPC Cation Channels

Identifiers

PMID19052171
PMCPMC2645922
OpenAlexW2141394516

What OpenQuestion holds

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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.