Evidence map›Paper›PMID 23476066›Full record

ReviewProceedings of the National Academy of Sciences of the United States of America2013

Stiffened lipid platforms at molecular force foci.

Andriy Anishkin, Ching Kung

Open access · bronzeAbstract readReview
In one paragraph

Review in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 40 papers.

0numbers the graph read from it
0cells of the map it votes in
40citing papers in PubMed
5.4field-weighted citation impact, top 3% 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

40 citing papers in PubMed, 91 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Review
  8. Mechanotransduction in gastrointestinal smooth muscle cells: role of mechanosensitive ion channels.American journal of physiology. Gastrointestinal and liver physiology · 2021
    Review
  9. Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. HowGenetics · 2019
    Review
  15. Article
  16. Remembering Mechanosensitivity of NMDA Receptors.Frontiers in cellular neuroscience · 2019
    Review
  17. Article
  18. Article
  19. Article
  20. Article
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

2 authors at 2 institutions in 1 country.

Andriy AnishkinDepartment of Biochemistry and Center for Computational Proteomics at the Huck Institute of Life Sciences, Pennsylvania State University, University Park, PA 16802, USA.
Ching Kung
Pennsylvania State University · USUniversity of Wisconsin–Madison · US

Funding

TRPV4: Mechanosensitivity and Skeletal DysplasiaR01GM096088 · NIGMS · UNIVERSITY OF WISCONSIN-MADISON · PI KUNG, CHING · 2011 to 2014
$1.1M
NIGMS NIH HHS GM096088NIGMS NIH HHS R01 GM096088
6 · The paper itself

Abstract

How mechanical forces are sensed remains largely mysterious. The forces that gate prokaryotic and several eukaryotic channels were found to come from the lipid membrane. Our survey of animal cells found that membrane force foci all have cholesterol-gathering proteins and are reinforced with cholesterol. This result is evident in overt force sensors at the tips of stereocilia for vertebrate hearing and the touch receptor of Caenorhabditis elegans and mammalian neurons. For less specialized cells, cadherins sustain the force between neighboring cells and integrins between cells and matrix. These tension bearers also pass through and bind to a cholesterol-enriched platform before anchoring to cytoskeleton through other proteins. Cholesterol, in alliance with sphingomyelin and specialized proteins, enforces a more ordered structure in the bilayer. Such a stiffened platform can suppress mechanical noise, redirect, rescale, and confine force. We speculate that such platforms may be dynamic. The applied force may allow disordered-phase lipids to enter the platform-staging channel opening in the thinner mobile neighborhood. The platform may also contain specialized protein/lipid subdomains enclosing mechanosensitive channels to open with localized tension. Such a dynamic stage can mechanically operate structurally disparate channels or enzymes without having to tie them directly to cadherin, integrin, or other protein tethers.

Indexed as

AnimalsCaenorhabditis elegansCholesterolCytoskeletonHumansMechanotransduction, CellularMembrane MicrodomainsMembrane ProteinsNeuronsSurface TensionCholesterolMembrane Proteins

Identifiers

PMID23476066
PMCPMC3612676
OpenAlexW2079046810

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.