Evidence map›Paper›PMID 41124252›Full record

ArticleScience advances2025

Cluster nanoarchitecture and structural diversity of PIEZO1 at rest and during activation in intact cells.

Clement Verkest, Lucas Roettger, Nadja Zeitzschel, James Hall, Oscar Sánchez-Carranza, Angela Tzu-Lun Huang, Gary R Lewin, Stefan G Lechner

Abstract read
In one paragraph

Article in Science advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
–field-weighted citation impact
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

7 citing papers in PubMed.

  1. Article
  2. Article
  3. Amoeboid cancer cells at a glance.Journal of cell science · 2026
    Review
  4. Piezo2 tension sensitivity and its modulation by alternative splicing.bioRxiv : the preprint server for biology · 2026
    Article
  5. Review
  6. Article
  7. 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

8 authors.

Clement VerkestDepartment of Anaesthesiology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.ORCID 0000-0001-8612-8002
Lucas RoettgerDepartment of Anaesthesiology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.ORCID 0009-0009-6112-0915
Nadja ZeitzschelDepartment of Anaesthesiology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.ORCID 0000-0003-4332-7049
James HallMax Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Molecular Physiology of Somatic Sensation Laboratory Berlin, Berlin, Germany.
Oscar Sánchez-CarranzaMax Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Molecular Physiology of Somatic Sensation Laboratory Berlin, Berlin, Germany.ORCID 0000-0002-8745-5176
Angela Tzu-Lun HuangMax Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Molecular Physiology of Somatic Sensation Laboratory Berlin, Berlin, Germany.ORCID 0000-0003-3471-192X
Gary R LewinMax Delbrück Center for Molecular Medicine in the Helmholtz Association (MDC), Molecular Physiology of Somatic Sensation Laboratory Berlin, Berlin, Germany.ORCID 0000-0002-2890-6352
Stefan G LechnerDepartment of Anaesthesiology, University Medical Center Hamburg-Eppendorf, Hamburg, Germany.ORCID 0000-0001-9402-9127

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The force-gated ion channel PIEZO1 confers mechanosensitivity to many cell types. While the structure and physiological roles of PIEZO1 are well-described, the subcellular distribution and the impact of the cellular microenvironment on PIEZO1 conformation and function are poorly understood. Here, using MINFLUX nanoscopy, we demonstrate that PIEZO1 channels accumulate in pit-shaped invaginations that are distinct from classical membrane invaginations such as clathrin-coated pits and caveolae, thereby possibly creating hotspots for mechanotransduction. Moreover, by measuring intramolecular distances in individual PIEZO1 channels with nanometer precision, we reveal subcellular compartment-specific differences in PIEZO1 conformation at rest and during activation that correlate with differences in PIEZO1 function and are possibly caused by differences in cytoskeletal architecture. Together, our data provide previously unrecognized insights into the complex interplay of forces that determine how PIEZO1 alters membrane shape and, vice versa, how the membrane together with the cytoskeleton affect the conformation and function of individual PIEZO1 channels.

Indexed as

Ion ChannelsAnimalsCell MembraneCytoskeletonHEK293 CellsHumansIon Channel GatingMechanotransduction, CellularProtein ConformationIon ChannelsPIEZO1 protein, human

Identifiers

PMID41124252
PMCPMC12542951

What Socratic holds

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LicenceCC BY-NC
Read underepoch 390

Registered trials

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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 Socratic graph.