*Result*: Cryo-light microscopy with angstrom precision deciphers structural conformations of PIEZO1 in its native state.

Title:
Cryo-light microscopy with angstrom precision deciphers structural conformations of PIEZO1 in its native state.
Authors:
Mazal H; Max Planck Institute for the Science of Light, 91058 Erlangen, Germany.; Max-Planck-Zentrum für Physik und Medizin, 91054 Erlangen, Germany., Wieser FF; Max Planck Institute for the Science of Light, 91058 Erlangen, Germany.; Max-Planck-Zentrum für Physik und Medizin, 91054 Erlangen, Germany.; Department of Physics, Friedrich-Alexander University of Erlangen-Nürnberg, 91058 Erlangen, Germany., Bollschweiler D; Max Planck Institute of Biochemistry, 82152 Planegg, Germany., Schambony A; Max Planck Institute for the Science of Light, 91058 Erlangen, Germany.; Max-Planck-Zentrum für Physik und Medizin, 91054 Erlangen, Germany.; Department of Biology, Friedrich-Alexander University of Erlangen-Nürnberg, 91058 Erlangen, Germany., Sandoghdar V; Max Planck Institute for the Science of Light, 91058 Erlangen, Germany.; Max-Planck-Zentrum für Physik und Medizin, 91054 Erlangen, Germany.; Department of Physics, Friedrich-Alexander University of Erlangen-Nürnberg, 91058 Erlangen, Germany.
Source:
Science advances [Sci Adv] 2025 Aug 22; Vol. 11 (34), pp. eadw4402. Date of Electronic Publication: 2025 Aug 20.
Publication Type:
Journal Article
Language:
English
Journal Info:
Publisher: American Association for the Advancement of Science Country of Publication: United States NLM ID: 101653440 Publication Model: Print-Electronic Cited Medium: Internet ISSN: 2375-2548 (Electronic) Linking ISSN: 23752548 NLM ISO Abbreviation: Sci Adv Subsets: MEDLINE
Imprint Name(s):
Original Publication: Washington, DC : American Association for the Advancement of Science, [2015]-
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Substance Nomenclature:
0 (Ion Channels)
0 (Piezo1 protein, mouse)
Entry Date(s):
Date Created: 20250820 Date Completed: 20250820 Latest Revision: 20250823
Update Code:
20260130
PubMed Central ID:
PMC12366687
DOI:
10.1126/sciadv.adw4402
PMID:
40834076
Database:
MEDLINE

*Further Information*

*Investigations based on cryo-electron microscopy (cryo-EM), atomic force microscopy, and super-resolution microscopy reveal a symmetric trimer with propeller-like blades for the mechanosensitive ion channel PIEZO. However, a conclusive understanding of its conformations in the cell membrane is lacking. Here, we implement a high-vacuum cryogenic shuttle to transfer shock-frozen cell membranes in and out of a cryostat designed for single-particle cryo-light microscopy (spCryo-LM). By localizing fluorescent labels placed at the extremities of the blades of the mouse PIEZO1 protein in unroofed cell membranes, we ascertain three configurations with radii of 6, 12, and 20 nanometers as projected onto the membrane plane. We elaborate on the correspondence of these data with previous reports in the literature. The combination of spCryo-LM with cryo-EM promises to provide quantitative insights into the structure and function of biomolecular complexes in their native environments without the need for chemical fixation or protein isolation, ushering in a new regime of correlative studies in structural biology.*