Evidence map›Paper›PMID 20208543›Full record

ArticleNature structural & molecular biology2010

The tension-transmitting 'clutch' in the mechanosensitive channel MscS.

Vladislav Belyy, Andriy Anishkin, Kishore Kamaraju, Naili Liu, Sergei Sukharev

Abstract read
PubMed Publisher
In one paragraph

Article in Nature structural & molecular biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.9field-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

46 citing papers in PubMed, 81 citations in OpenAlex.

  1. The MscS channel frombioRxiv : the preprint server for biology · 2026
    Article
  2. Article
  3. Article
  4. Article
  5. Review
  6. Article
  7. Cyclodextrins increase membrane tension and are universal activators of mechanosensitive channels.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  8. Mechanosensitive channel gating by delipidation.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Tissue mechanics govern the rapidly adapting and symmetrical response to touch.Proceedings of the National Academy of Sciences of the United States of America · 2015
    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

5 authors at 1 institution in 1 country.

Vladislav BelyyDepartment of Biology, University of Maryland College Park, College Park, Maryland, USA.
Andriy Anishkin
Kishore Kamaraju
Naili Liu
Sergei Sukharev
University of Maryland, College Park · US

Funding

Howard Hughes Medical Institute
6 · The paper itself

Abstract

Under prolonged stimulation, the mechanosensitive channel MscS of Escherichia coli enters a tension-insensitive inactivated state. We transformed the delipidated crystal structure and restored the link between lipid-facing TM1 and TM2 and gate-forming TM3 helices. Joining the conserved Phe68 of TM2 with Leu111 of TM1, this buried contact mediated opening in steered molecular dynamics simulations with forces applied to the peripheral helices. Both F68S and L111S substitutions produced severe loss-of-function phenotypes in vivo by increasing the inactivation rate and promoting unusual 'silent' inactivation from the resting state. F68S also suppressed the noninactivating phenotype of G113A. The L111C cysteine buried in the TM2-TM3 crevice was accessible to methanethiosulfonate-ethyltrimethylammonium (MTSET) only in the inactivated state, which was stabilized upon modification by a positive charge. The restored interhelical contact thus is critically involved in force transmission from the lipid-facing helices to the gate, and inactivation appears to be a result of TM2-TM3 uncoupling.

Indexed as

Escherichia coliEscherichia coli ProteinsIon ChannelsModels, MolecularMolecular Dynamics SimulationProtein ConformationEscherichia coli ProteinsIon ChannelsMscS protein, E coli

Identifiers

PMID20208543
OpenAlexW2090973569

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.