Evidence map›Paper›PMID 19219385›Full record

ArticleThe Journal of membrane biology2009

Mechanical force and cytoplasmic Ca(2+) activate yeast TRPY1 in parallel.

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

Abstract read
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In one paragraph

Article in The Journal of membrane biology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

19 citing papers in PubMed, 36 citations in OpenAlex.

  1. Article
  2. Calcium Ion Channels inJournal of fungi (Basel, Switzerland) · 2023
    Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Calcium signaling and copper toxicity in Saccharomyces cerevisiae cells.Environmental science and pollution research international · 2016
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Review
  18. Review
  19. The use of yeast to understand TRP-channel mechanosensitivity.Pflugers Archiv : European journal of physiology · 2009
    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

5 authors at 1 institution in 1 country.

Zhenwei SuUniversity of Wisconsin-Madison, 53706, USA.
Xinliang Zhou
Stephen H Loukin
Yoshiro Saimi
Ching Kung
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
NIGMS NIH HHS GM47856NIGMS NIH HHS GM54867
6 · The paper itself

Abstract

The ability to sense mechanical and osmotic stimuli is vital to all organisms from mammals to bacteria. Members of the transient receptor potential (TRP) ion-channel family have attracted intense attention for their involvement in mechanosensation. The yeast homologue TRPY1 can clearly be activated by hypertonic shock in vivo and by stretch force under patch clamp. Like its animal counterparts, TRPY1 is polymodal, being gated by membrane stretch force and by cytoplasmic Ca(2+). Here, we investigated how these two gating principles interact. We found that stretch force can induce some channel activation without cytoplasmic Ca(2+). Tens of micromolar Ca(2+) greatly enhance the observed force-induced activities, with open probabilities following well the Boltzmann distribution, in which the two gating energies are summed as exponents. To map this formalism to structures, we found Ca(2+)-binding proteins such as calmodulin or calcineurin to be unnecessary. However, removing a dense cluster of negative charges in the C-terminal cytoplasmic domain of TRPY1 greatly diminishes the Ca(2+) activation as well as its influence on force activation. We also found a strategic point upstream of this charge cluster, at which insertion of amino acids weakens Ca(2+) activation considerably but leaves the mechanosensitivity nearly intact. These results led to a structure-function model in which Ca(2+) binding to the cytoplasmic domain and stretching of the membrane-embedded domain both generate gating force, reaching the gate in parallel.

Indexed as

Biomechanical PhenomenaCalcineurinCalciumCalmodulinCytoplasmElectrophysiologyMutagenesis, Site-DirectedPatch-Clamp TechniquesSaccharomyces cerevisiae ProteinsTransient Receptor Potential ChannelsCalcineurinCalciumCalmodulinSaccharomyces cerevisiae ProteinsTransient Receptor Potential Channels

Identifiers

PMID19219385
OpenAlexW2145700525

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.