Evidence map›Paper›PMID 28905417›Full record

ArticleProteins2017

Investigating the structural dynamics of the PIEZO1 channel activation and inactivation by coarse-grained modeling.

Wenjun Zheng, Frederick Sachs

Open access · greenAbstract read
In one paragraph

Article in Proteins, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
0.3field-weighted citation impact, top 38% 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

2 citing papers in PubMed, 9 citations in OpenAlex.

  1. Article
  2. Mechanisms of PIEZO Channel Inactivation.International journal of molecular sciences · 2023
    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

2 authors at 1 institution in 1 country.

Wenjun ZhengDepartment of Physics, State University of New York at Buffalo, Buffalo, New York.ORCID http://orcid.org/0000-0002-6236-9765
Frederick SachsDepartment of Physiology and Biophysics, State University of New York at Buffalo, Buffalo, New York.
University at Buffalo, State University of New York · US

Funding

University of Buffalo Clinical and Translational Science Institute - Supplement SchulyerUL1TR001412 · NCATS · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI MURPHY, TIMOTHY F · 2015 to 2024
$33.8M
Mechanosensitive ion channels and cortical mechanicsR01HL054887 · NHLBI · STATE UNIVERSITY OF NEW YORK AT BUFFALO · PI SACHS, FREDERICK · 1995 to 2016
$9.6M
NCATS NIH HHS UL1 TR001412NHLBI NIH HHS R01 HL054887
6 · The paper itself

Abstract

The PIEZO channels, a family of mechanosensitive channels in vertebrates, feature a fast activation by mechanical stimuli (eg, membrane tension) followed by a slower inactivation. Although a medium-resolution structure of the trimeric form of PIEZO1 was solved by cryo-electron microscopy (cryo-EM), key structural changes responsible for the channel activation and inactivation are still unknown. Toward decrypting the structural mechanism of the PIEZO1 activation and inactivation, we performed systematic coarse-grained modeling using an elastic network model and related modeling/analysis tools (ie, normal mode analysis, flexibility and hotspot analysis, correlation analysis, and cryo-EM-based hybrid modeling and flexible fitting). We identified four key motional modes that may drive the tension-induced activation and inactivation, with fast and slow relaxation time, respectively. These modes allosterically couple the lateral and vertical motions of the peripheral domains to the opening and closing of the intra-cellular vestibule, enabling external mechanical forces to trigger, and regulate the activation/inactivation transitions. We also calculated domain-specific flexibility profiles, and predicted hotspot residues at key domain-domain interfaces and hinges. Our results offer unprecedented structural and dynamic information, which is consistent with the literature on mutational and functional studies of the PIEZO channels, and will guide future studies of this important family of mechanosensitive channels.

Indexed as

Mechanotransduction, CellularBiomechanical PhenomenaCryoelectron MicroscopyHumansIon ChannelsMolecular Dynamics SimulationPliabilityProtein Interaction Domains and MotifsProtein MultimerizationProtein Structure, SecondaryIon ChannelsPIEZO1 protein, humanactivationcoarse-grained modelingcorrelation analysiscryo-EMelastic network modelflexible fittinghotspot residuesinactivationnormal mode analysisPIEZOtransition pathways

Identifiers

PMID28905417
PMCPMC5758363
OpenAlexW2755752129

What OpenQuestion holds

Textmetadata
LicenceTDM
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.