ArticleThe Journal of biological chemistry
Identification and functional characterization of the Piezo1 channel pore domain.
Article in The Journal of biological chemistry. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed.
- Noninvasive biophysical modulations of Piezo ion channels.Microsystems & nanoengineering · 2026Review
- PIEZO1 variants that reduce open channel probability are associated with familial osteoarthritis.The Journal of biological chemistry · 2026Article
- Insulin facilitates entry of calcium ions into human and murine erythrocytes via Piezo1: a newly identified mechanism with implications for type 2 diabetes.The FEBS journal · 2025Article
- The Mechanosensitive PIEZO1 Channel Contributes to the Reaction of RAW264.7 Macrophages to Mechanical Strain.Mediators of inflammation · 2025Article
- Mechanotransduction of Piezo1 in the cancer microenvironment: implications for NK cell-based immunotherapy.Frontiers in oncology · 2025Review
- Piezo in the eye: expression, distribution and roles in ocular diseases.Frontiers in physiology · 2025Review
- Piezo1, the new actor in cell volume regulation.Pflugers Archiv : European journal of physiology · 2024Review
- PIEZO1 loss-of-function compound heterozygous mutations in the rare congenital human disorder Prune Belly Syndrome.Nature communications · 2024Article
- Structural and thermodynamic framework for PIEZO1 modulation by small molecules.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Force-induced motions of the PIEZO1 blade probed with fluorimetry.Cell reports · 2023Article
- Microscopic mechanism of PIEZO1 activation by pressure-induced membrane stretch.The Journal of general physiology · 2023Article
- Optical control of PIEZO1 channels.Nature communications · 2023Article
- Yoda1's energetic footprint on Piezo1 channels and its modulation by voltage and temperature.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Piezo1-Regulated Mechanotransduction Controls Flow-Activated Lymphatic Expansion.Circulation research · 2022Article
- The anchor domain is critical for Piezo1 channel mechanosensitivity.Channels (Austin, Tex.) · 2021Article
- Roles of mechanosensitive channel Piezo1/2 proteins in skeleton and other tissues.Bone research · 2021Review
- Selective Chemical Activation of Piezo1 in Leukemia Cell Membrane: Single Channel Analysis.International journal of molecular sciences · 2021Article
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Authors and funding
3 authors.
Funding
Abstract
Mechanotransduction is the process by which cells convert physical forces into electrochemical responses. On a molecular scale, these forces are detected by mechanically activated ion channels, which constitute the basis for hearing, touch, pain, cold, and heat sensation, among other physiological processes. Exciting high-resolution structural details of these channels are currently emerging that will eventually allow us to delineate the molecular determinants of gating and ion permeation. However, our structural-functional understanding across the family remains limited. Piezo1 is one of the largest and least understood of these channels, with various structurally identified features within its trimeric assembly. This study seeks to determine the modularity and function of Piezo1 channels by constructing deletion proteins guided by cryo EM structural knowledge. Our comprehensive functional study identified, for the first time, the minimal amino acid sequence of the full-length Piezo1 that can fold and function as the channel's pore domain between E2172 and the last residue E2547. While the addition of an anchor region has no effect on permeation properties. The Piezo1 pore domain is not pressure-sensitive and the appending of Piezo Repeat-A did not restore pressure-dependent gating, hence the sensing module must exist between residues 1 to 1952. Our efforts delineating the permeation and gating regions within this complex ion channel have implications in identifying small molecules that exclusively regulate the activity of the channel's pore module to influence mechanotransduction and downstream processes.
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