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- PDB-11ye: Curved structure of mPiezo1 in plasma membrane vesicles -

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Basic information

Entry
Database: PDB / ID: 11ye
TitleCurved structure of mPiezo1 in plasma membrane vesicles
ComponentsPiezo-type mechanosensitive ion channel component 1
KeywordsMEMBRANE PROTEIN / Piezo1 / ion channel / mechanosensitive
Function / homology
Function and homology information


mechanosensitive monoatomic cation channel activity / cuticular plate / positive regulation of integrin activation / detection of mechanical stimulus / positive regulation of cell-cell adhesion mediated by integrin / mechanosensitive monoatomic ion channel activity / stereocilium / positive regulation of myotube differentiation / lamellipodium membrane / monoatomic cation transport ...mechanosensitive monoatomic cation channel activity / cuticular plate / positive regulation of integrin activation / detection of mechanical stimulus / positive regulation of cell-cell adhesion mediated by integrin / mechanosensitive monoatomic ion channel activity / stereocilium / positive regulation of myotube differentiation / lamellipodium membrane / monoatomic cation transport / monoatomic cation channel activity / endoplasmic reticulum-Golgi intermediate compartment membrane / cellular response to mechanical stimulus / regulation of membrane potential / endoplasmic reticulum membrane / endoplasmic reticulum / identical protein binding / plasma membrane
Similarity search - Function
Piezo family / Piezo non-specific cation channel, R-Ras-binding domain / Piezo domain / : / : / : / Piezo non-specific cation channel, cap domain / Piezo TM25-28 / Piezo1-like, transmembrane helical unit / Piezo TM1-24 / Piezo, THU9 and anchor domain
Similarity search - Domain/homology
Piezo-type mechanosensitive ion channel component 1
Similarity search - Component
Biological speciesMus musculus (house mouse)
MethodELECTRON MICROSCOPY / single particle reconstruction / cryo EM / Resolution: 3.7 Å
AuthorsVaisey, G.V. / MacKinnon, R.M.
Funding support United States, 1items
OrganizationGrant numberCountry
Howard Hughes Medical Institute (HHMI) United States
CitationJournal: Sci Adv / Year: 2026
Title: Lipid composition and mechanical force underlie multi-modal regulation of Piezo1 gating.
Authors: George Vaisey / Roderick MacKinnon /
Abstract: Piezo1 ion channels are widely expressed cellular mechanosensors. They adopt an intrinsically curved shape when closed and are thought to open when mechanical forces applied to the membrane favor a ...Piezo1 ion channels are widely expressed cellular mechanosensors. They adopt an intrinsically curved shape when closed and are thought to open when mechanical forces applied to the membrane favor a more flattened conformation. In previous studies, Piezo1 channels in lipid vesicles adopted a somewhat flattened conformation mediated by membrane curvature; however, the ion conduction pore remained closed. In line with the closed pore, Piezo1 channels do not open and conduct ions in the kind of lipids that were used in the structural studies. Here, we show first that Piezo1 channels in cell-derived membranes retain the ability to open and conduct ions under mechanical force, and second, that in cell-derived membrane vesicles, they adopt a more completely flattened disk shape associated with large conformational changes within and around the ion conduction pathway. These conformational changes occurring in cell-derived lipid membranes suggest that mechanical force is necessary but insufficient, and that a specific membrane-derived cofactor complements mechanical force to activate Piezo1.
History
DepositionMar 18, 2026Deposition site: RCSB / Processing site: RCSB
Revision 1.0Apr 29, 2026Provider: repository / Type: Initial release
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Structure visualization

Structure viewerMolecule:
MolmilJmol/JSmol

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Assembly

Deposited unit
C: Piezo-type mechanosensitive ion channel component 1
D: Piezo-type mechanosensitive ion channel component 1
E: Piezo-type mechanosensitive ion channel component 1


Theoretical massNumber of molelcules
Total (without water)882,2423
Polymers882,2423
Non-polymers00
Water00
1


  • Idetical with deposited unit
  • defined by author&software
  • Evidence: electron microscopy, not applicable
TypeNameSymmetry operationNumber
identity operation1_555x,y,z1
MethodPISA

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Components

#1: Protein Piezo-type mechanosensitive ion channel component 1 / Protein FAM38A


Mass: 294080.688 Da / Num. of mol.: 3
Source method: isolated from a genetically manipulated source
Source: (gene. exp.) Mus musculus (house mouse) / Gene: Piezo1, Fam38a / Production host: Homo sapiens (human) / References: UniProt: E2JF22
Has protein modificationY

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Experimental details

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Experiment

ExperimentMethod: ELECTRON MICROSCOPY
EM experimentAggregation state: PARTICLE / 3D reconstruction method: single particle reconstruction

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Sample preparation

ComponentName: mousePiezo1 / Type: COMPLEX / Entity ID: all / Source: RECOMBINANT
Source (natural)Organism: Mus musculus (house mouse)
Source (recombinant)Organism: Homo sapiens (human) / Strain: expi293 F cells
Buffer solutionpH: 8
SpecimenEmbedding applied: NO / Shadowing applied: NO / Staining applied: NO / Vitrification applied: YES
VitrificationCryogen name: ETHANE

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Electron microscopy imaging

Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company
MicroscopyModel: TFS KRIOS
Electron gunElectron source: FIELD EMISSION GUN / Accelerating voltage: 300 kV / Illumination mode: FLOOD BEAM
Electron lensMode: BRIGHT FIELD / Nominal defocus max: 2000 nm / Nominal defocus min: 1000 nm
Image recordingElectron dose: 60 e/Å2 / Film or detector model: FEI FALCON IV (4k x 4k)

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Processing

EM software
IDNameCategory
1Topazparticle selection
5cryoSPARC3D reconstruction
CTF correctionType: PHASE FLIPPING AND AMPLITUDE CORRECTION
3D reconstructionResolution: 3.7 Å / Resolution method: FSC 0.143 CUT-OFF / Num. of particles: 69370 / Symmetry type: POINT
RefinementHighest resolution: 3.7 Å

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