Evidence map›Paper›PMID 20605796›Full record

ArticleThe Journal of biological chemistry2010

Wild-type and brachyolmia-causing mutant TRPV4 channels respond directly to stretch force.

Stephen Loukin, Xinliang Zhou, Zhenwei Su, Yoshiro Saimi, Ching Kung

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 88 papers.

0numbers the graph read from it
0cells of the map it votes in
88citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

88 citing papers in PubMed, 154 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Review
  10. Mechanosensing by Vascular Endothelium.Annual review of physiology · 2024
    Review
  11. Article
  12. Mechanosensory entities and functionality of endothelial cells.Frontiers in cell and developmental biology · 2024
    Review
  13. Article
  14. Article
  15. Article
  16. Ion Channels in the Development and Remodeling of the Aortic Valve.International journal of molecular sciences · 2023
    Review
  17. Article
  18. Article
  19. Article
  20. Article

28 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 1 institution in 1 country.

Stephen LoukinLaboratory of Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706. Electronic address: shloukin@wisc.edu.
Xinliang ZhouLaboratory of Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706.
Zhenwei SuLaboratory of Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706.
Yoshiro SaimiLaboratory of Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706.
Ching KungLaboratory of Molecular Biology, University of Wisconsin, Madison, Wisconsin 53706; Department of Genetics, University of Wisconsin, Madison, Wisconsin 53706.
University of Wisconsin–Madison · US

Funding

Study of mechanosensation using microbial TRP channelsR01GM047856 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 1994 to 2008
$2.2M
Molecular Basis of Hypertonicity Sensing by Yeast Yvc1pR01GM054867 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 1998 to 2010
$2.2M
Reconstituting Purified Rat TRPV4 in Lipid Bilayer to Test Its MechanosensitivityR03NS067360 · NINDS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 2009 to 2010
$148k
NIGMS NIH HHS GM047856NIGMS NIH HHS GM054867NIGMS NIH HHS R01 GM047856NIGMS NIH HHS R01 GM054867NINDS NIH HHS NS067360NINDS NIH HHS R03 NS067360
6 · The paper itself

Abstract

Whether animal ion channels functioning as mechanosensors are directly activated by stretch force or indirectly by ligands produced by the stretch is a crucial question. TRPV4, a key molecular model, can be activated by hypotonicity, but the mechanism of activation is unclear. One model has this channel being activated by a downstream product of phospholipase A(2), relegating mechanosensitivity to the enzymes or their regulators. We expressed rat TRPV4 in Xenopus oocytes and repeatedly examined >200 excised patches bathed in a simple buffer. We found that TRPV4 can be activated by tens of mm Hg pipette suctions with open probability rising with suction even in the presence of relevant enzyme inhibitors. Mechanosensitivity of TRPV4 provides the simplest explanation of its various force-related physiological roles, one of which is in the sensing of weight load during bone development. Gain-of-function mutants cause heritable skeletal dysplasias in human. We therefore examined the brachyolmia-causing R616Q gain-of-function channel and found increased whole-cell current densities compared with wild-type channels. Single-channel analysis revealed that R616Q channels maintain mechanosensitivity but have greater constitutive activity and no change in unitary conductance or rectification.

Indexed as

Mutation, MissenseAnimalsBone Diseases, DevelopmentalDisease Models, AnimalGenetic Diseases, InbornHumansOocytesPhospholipases A2RatsTRPV Cation ChannelsWeight-BearingXenopusPhospholipases A2TRPV4 protein, humanTrpv4 protein, ratTRPV Cation Channels

Identifiers

PMID20605796
PMCPMC2930716
OpenAlexW1982319165

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.