Evidence map›Paper›PMID 31968259›Full record

ArticleCell reports2020

Inactivation Kinetics and Mechanical Gating of Piezo1 Ion Channels Depend on Subdomains within the Cap.

Amanda H Lewis, Jörg Grandl

Registry-linked trialOpen access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It is linked to trial NCT06052631 (Microneurographic Assessment of Peripheral Nerves in Healthy Volunteers and Individuals With Sensory Dysfunction Caused by Inherited Mutations in the PIEZO2 Gene), which is not on this map. Cited by 59 papers.

0numbers the graph read from it
0cells of the map it votes in
59citing 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.

NCT06052631 not yet recruitingnot on this mapstarted 2026, after this paper: background citation

Microneurographic Assessment of Peripheral Nerves in Healthy Volunteers and Individuals With Sensory Dysfunction Caused by Inherited Mutations in the PIEZO2 Gene

TypeobservationalSponsorNational Center for Complementary and Integrative Health (NCCIH)Ran2026 to 2026Enrolled16ConditionsPIEZO2-Deficiency Syndrome
3 · Its place in the literature

Who cites it

59 citing papers in PubMed, 83 citations in OpenAlex.

  1. Review
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Lipid Regulation of Mechanosensitive Ion Channels.International journal of molecular sciences · 2026
    Review
  11. Article
  12. Review
  13. Review
  14. PIEZO1 in Immune Cells: From Force to Function.Results and problems in cell differentiation · 2026
    Review
  15. Review
  16. 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 1 institution in 1 country.

Amanda H LewisDepartment of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA.
Jörg GrandlDepartment of Neurobiology, Duke University Medical Center, Durham, NC 27710, USA. Electronic address: grandl@neuro.duke.edu.
Duke Medical Center · US

Funding

Mechanisms of Disease associated with mechanically-activated Piezo ion channelsR01NS110552 · NINDS · DUKE UNIVERSITY · PI GRANDL, JORG · 2020 to 2024
$1.8M
The mechanism of temperature-activation of TRP ion channelsR01NS088402 · NINDS · DUKE UNIVERSITY · PI GRANDL, JORG · 2015 to 2019
$1.7M
Identifying the physical stimuli for activation and sensitization of Piezo mechanosensitive ion channelsF32NS094088 · NINDS · DUKE UNIVERSITY · PI LEWIS, AMANDA HALLEY · 2016 to 2018
$179k
NINDS NIH HHS F32 NS094088NINDS NIH HHS R01 NS088402NINDS NIH HHS R01 NS110552
6 · The paper itself

Abstract

Piezo1 ion channels are activated by mechanical stimuli and mediate the sensing of blood flow. Although cryo-electron microscopy (cryo-EM) structures have revealed the overall architecture of Piezo1, the precise domains involved in activation and subsequent inactivation have remained elusive. Here, we perform a targeted chimeric screen between Piezo1 and the closely related isoform Piezo2 and use electrophysiology to characterize their inactivation kinetics during mechanical stimulation. We identify three small subdomains within the extracellular cap that individually can confer the distinct kinetics of inactivation of Piezo2 onto Piezo1. We further show by cysteine crosslinking that conformational flexibility of these subdomains is required for mechanical activation to occur and that electrostatic interactions functionally couple the cap to the extensive blades, which have been proposed to function as sensors of membrane curvature and tension. This study provides a demonstration of internal gating motions involved in mechanotransduction by Piezo1.

Indexed as

Ion Channel GatingAmino AcidsAnimalsCross-Linking ReagentsHEK293 CellsHumansIon ChannelsKineticsMechanotransduction, CellularMiceProtein DomainsStatic ElectricityStructure-Activity RelationshipAmino AcidsCross-Linking ReagentsIon ChannelsPIEZO1 protein, humanPiezo1 protein, mouseactivationgatinginactivationmechanosensitive ion channelmechanotransductionPiezo1Piezo2

Identifiers

PMID31968259
PMCPMC7021530
OpenAlexW3001537456

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
Read underepoch 390

Registered trials

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.