Evidence map›Paper›PMID 23948741›Full record

ArticlePflugers Archiv : European journal of physiology2014

Isoform- and receptor-specific channel property of canonical transient receptor potential (TRPC)1/4 channels.

Jinsung Kim, Misun Kwak, Jae-Pyo Jeon, Jongyun Myeong, Jinhong Wie, Chansik Hong, Sung-Young Kim, Ju-Hong Jeon, Hyun Jin Kim, Insuk So

Erratum issuedAbstract read
PubMed Publisher
In one paragraph

Article in Pflugers Archiv : European journal of physiology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 25 papers.

0numbers the graph read from it
0cells of the map it votes in
25citing papers in PubMed
1.5field-weighted citation impact, top 22% 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

25 citing papers in PubMed, 40 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. 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
  6. Article
  7. Molecular architecture of the GαNature communications · 2023
    Article
  8. Review
  9. Distribution and Assembly of TRP Ion Channels.Advances in experimental medicine and biology · 2021
    Article
  10. Review
  11. Review
  12. Article
  13. Review
  14. TRPC1 as a negative regulator for TRPC4 and TRPC5 channels.Pflugers Archiv : European journal of physiology · 2019
    Review
  15. Differential PI(4,5)PScientific reports · 2019
    Article
  16. Review
  17. Dual action of the GαScientific reports · 2018
    Article
  18. Article
  19. Article
  20. Calcium permeability of transient receptor potential canonical (TRPC) 4 channels measured by TRPC4-GCaMP6s.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2017
    Article
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

10 authors at 3 institutions in 1 country.

Jinsung KimDepartment of Chemistry, Korea Advanced Institute of Science and Technology, Daejeon, 305-701, Republic of Korea.
Misun Kwak
Jae-Pyo Jeon
Jongyun Myeong
Jinhong Wie
Chansik Hong
Sung-Young Kim
Ju-Hong Jeon
Hyun Jin Kim
Insuk So
Seoul National University · KRKorea Advanced Institute of Science and Technology · KRSungkyunkwan University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Transient receptor potential canonical (TRPC) 1, the first mammalian homologue of Drosophila trp gene, is distributed widely in mammalian cells and is involved in many physiological functions. TRPC1 is reported to be functional following heteromeric formation with other TRPC channels such as TRPC4 or TRPC5. It is known that the composition of this widely distributed TRPC1 is far from simple; functionality of such channels has been highly controversial. Furthermore, TRPC1 gene is known to have two splicing variants; one encodes long (TRPC1α) and the other encodes short (TRPC1β) TRPC1 isoforms, respectively. In this study, we examined the functionality of TRPC1/4 channels using various activation systems. Gq/11-coupled receptor (e.g., M1 or M3 receptors) stimulation significantly increased TRPC1α/4 currents but induced mild activation of TRPC1β/4. In addition, when expressed with TRPC4, TRPC1α acted as a pore-constituting subunit and not a β ancillary subunit. Multimerized with TRPC4, TRPC1α also generated strong pore field strength. We also found that Gi/o-coupled receptor (e.g., M2 receptor) stimulation was insufficient to activate TRPC1α/4 and TRPC1β/4 channels but selectively activated TRPC4 homomeric channels. These findings demonstrate that TRPC1/4 channel shows dynamic gating property depending on TRPC1 isoform subtypes and receptor stimulation system. Therefore, careful discrimination of the specificity of TRPC1 isoforms and upstream activation system is important in thorough understanding of TRPC1 and TRPC1/4 channels.

Indexed as

Protein MultimerizationAction PotentialsAmino Acid SequenceHEK293 CellsHumansMolecular Sequence DataProtein BindingProtein IsoformsProtein TransportReceptor, Muscarinic M2TRPC Cation ChannelsProtein IsoformsReceptor, Muscarinic M2transient receptor potential cation channel, subfamily C, member 1TRPC4 ion channelTRPC Cation Channels

Identifiers

PMID23948741
OpenAlexW1975389562

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.