Evidence map›Paper›PMID 22157757›Full record

ArticleThe Journal of biological chemistry2012

Transient receptor potential channel 1 (TRPC1) reduces calcium permeability in heteromeric channel complexes.

Ursula Storch, Anna-Lena Forst, Maximilian Philipp, Thomas Gudermann, Michael Mederos y Schnitzler

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 95 papers.

0numbers the graph read from it
0cells of the map it votes in
95citing papers in PubMed
4.7field-weighted citation impact, top 4% 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

95 citing papers in PubMed, 143 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Cryo-EM structure of the heteromeric TRPC1/TRPC4 channel.Nature structural & molecular biology · 2025
    Article
  7. The mutual interaction of TRPC5 channel with polycystin proteins.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2025
    Article
  8. Article
  9. Article
  10. TRP Channels in Stroke.Neuroscience bulletin · 2024
    Review
  11. Review
  12. Article
  13. Review
  14. Review
  15. Article
  16. Transient Receptor Potential (TRP) Channels in Tumor Vascularization.International journal of molecular sciences · 2022
    Review
  17. Article
  18. Review
  19. TRPC channels as emerging targets for seizure disorders.Trends in pharmacological sciences · 2022
    Review
  20. Article

35 more citing papers are in PubMed but not listed here.

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 2 institutions in 1 country.

Ursula StorchWalther-Straub-Institute for Pharmacology and Toxicology, Ludwig-Maximilians University, 80336 Munich, Germany.
Anna-Lena Forst
Maximilian Philipp
Thomas Gudermann
Michael Mederos y Schnitzler
Ludwig-Maximilians-Universität München · DEPhilipps University of Marburg · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Specific biological roles of the classical transient receptor potential channel 1 (TRPC1) are still largely elusive. To investigate the function of TRPC1 proteins in cell physiology, we studied heterologously expressed TRPC1 channels and found that recombinant TRPC1 subunits do not form functional homomeric channels. Instead, by electrophysiological analysis TRPC1 was shown to form functional heteromeric, receptor-operated channel complexes with TRPC3, -4, -5, -6, and -7 indicating that TRPC1 proteins can co-assemble with all members of the TRPC subfamily. In all TRPC1-containing heteromers, TRPC1 subunits significantly decreased calcium permeation. The exchange of select amino acids in the putative pore-forming region of TRPC1 further reduced calcium permeability, suggesting that TRPC1 subunits contribute to the channel pore. In immortalized immature gonadotropin-releasing hormone neurons endogenously expressing TRPC1, -2, -5, and -6, down-regulation of TRPC1 resulted in increased calcium permeability and elevated basal cytosolic calcium concentrations. We did not observe any involvement of TRPC1 in store-operated cation influx. Notably, TRPC1 suppressed the migration of gonadotropin-releasing hormone neurons without affecting cell proliferation. Conversely, in TRPC1 knockdown neurons, specific migratory properties like distance covered, locomotion speed, and directionality were increased. These findings suggest a novel regulatory mechanism relying on the expression of TRPC1 and the subsequent formation of heteromeric TRPC channel complexes with reduced calcium permeability, thereby fine-tuning neuronal migration.

Indexed as

AnimalsCalciumCell MovementCHO CellsCricetinaeCricetulusGene Expression RegulationGene Knockdown TechniquesGonadotropin-Releasing HormoneHEK293 CellsHumansMiceNeuronsPermeabilityProtein Structure, QuaternaryRatsCalciumGonadotropin-Releasing Hormonetransient receptor potential cation channel, subfamily C, member 1TRPC3 cation channelTRPC4 ion channelTRPC5 protein, humanTrpc5 protein, mouseTrpc5 protein, ratTRPC6 Cation ChannelTRPC6 protein, humanTRPC Cation Channels

Identifiers

PMID22157757
PMCPMC3271006
OpenAlexW1995239231

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.