Evidence map›Paper›PMID 20682256›Full record

ArticleBiophysical journal2010

Atomic force microscopy reveals the alternating subunit arrangement of the TRPP2-TRPV4 heterotetramer.

Andrew P Stewart, Graham D Smith, Richard N Sandford, J Michael Edwardson

Open access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 51 papers.

0numbers the graph read from it
0cells of the map it votes in
51citing papers in PubMed
4.5field-weighted citation impact, top 5% 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

51 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
  2. Review
  3. Review
  4. Article
  5. TRPP2 is located in the primary cilia of human non-pigmented ciliary epithelial cells.Graefe's archive for clinical and experimental ophthalmology = Albrecht von Graefes Archiv fur klinische und experimentelle Ophthalmologie · 2024
    Article
  6. Review
  7. Article
  8. Article
  9. Endothelial TRPV4 channels in lung edema and injury.Current topics in membranes · 2022
    Review
  10. Review
  11. CaCells · 2021
    Review
  12. Review
  13. TRPing on Cell Swelling - TRPV4 Senses It.Frontiers in immunology · 2021
    Review
  14. Distribution and Assembly of TRP Ion Channels.Advances in experimental medicine and biology · 2021
    Article
  15. Review
  16. Article
  17. Review
  18. TRPV4: A Physio and Pathophysiologically Significant Ion Channel.International journal of molecular sciences · 2020
    Review
  19. Review
  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

4 authors at 1 institution in 1 country.

Andrew P StewartDepartment of Pharmacology, University of Cambridge, Cambridge, United Kingdom.
Graham D Smith
Richard N Sandford
J Michael Edwardson
University of Cambridge · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

There is evidence that polycystin-2 (TRPP2) interacts with two other members of the transient receptor potential (TRP) family, TRPC1 and TRPV4. We have previously shown that TRPP2 forms a heteromeric complex with TRPC1, with a 2:2 stoichiometry and an alternating subunit arrangement. Here, we used coimmunoprecipitation to show that TRPP2 also interacts with TRPV4, but not with TRPA1 or TRPM8; hence, its promiscuity is limited. We then used atomic force microscopy to study the structure of the TRPV4 homomer and the interaction between TRPP2 and TRPV4. The molecular volume of V5-tagged TRPV4 isolated from singly-transfected tsA 201 cells indicated that it assembled as a homotetramer. The distribution of angles between pairs of anti-V5 antibodies bound to TRPV4 particles had a large peak close to 90 degrees and a smaller peak close to 180 degrees , again consistent with the assembly of TRPV4 as a homotetramer. In contrast, the angle distributions for decoration of the TRPP2-TRPV4 heteromer by either anti-Myc or anti-V5 antibodies had major peaks close to 180 degrees. This result indicates that TRPP2-TRPV4 assembles identically to TRPP2-TRPC1, suggesting a common subunit arrangement among heteromeric TRP channels.

Indexed as

Microscopy, Atomic ForceProtein MultimerizationAnimalsCell LineHumansImmunoprecipitationMiceProtein SubunitsRatsTRPP Cation ChannelsTRPV Cation ChannelsProtein SubunitsTRPP Cation ChannelsTrpv4 protein, mouseTRPV Cation Channels

Identifiers

PMID20682256
PMCPMC2913176
OpenAlexW2022253437

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.